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Chapter 1 : Structure and Function of Prokaryotic and Eukaryotic Cells

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Abstract:

This chapter provides an overview of the basic concepts of eukaryotic and prokaryotic cell structure and function. The practical importance of each topic is described in the context of understanding the invasion of eukaryotic hosts by pathogenic bacterial cells. Eukaryotic cells are generally 10 to 100 µm in diameter and thus have 103 to 106 times the volume of typical prokaryotic cells. Organelles commonly found in animal cells include the nucleus, the endoplasmic reticulum, the Golgi apparatus, lysosomes, the mitochondria, peroxisomes, and ribosomes. The outer membrane of gram-negative bacteria provides structures and receptors that affect adhesion to host cells, resistance to phagocytosis, and susceptibility to bacteriophages. Bacteria occur as single cells or as cell associations. The bacterial cell wall is a unique structure which surrounds the cytoplasmic membrane. Bacterial cell walls are constructed from a variety of macromolecules and polymers. Structurally, the wall is necessary for maintaining the cell’s characteristic shape and countering the effect of osmotic pressure. Peptidoglycan (or murein) is a cross-linked biopolymer. The nucleoid is the site of DNA and RNA synthesis. The chromosome is the main genomic element of bacteria as a single larger circular DNA molecule. It contains the genes for all "essential" functions and structures of the bacterial cell.

Citation: Mascaretti O. 2003. Structure and Function of Prokaryotic and Eukaryotic Cells, p 1-32. In Bacteria versus Antibacterial Agents. ASM Press, Washington, DC. doi: 10.1128/9781555817794.ch1
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Image of Figure 1.1
Figure 1.1

Structure of a representative animal cell. Reprinted from G. M. Cooper, The Cell: a Molecular Approach (ASM Press, Washington, D.C., and Sinauer Associates, Inc.,Sunderland, Mass., 2000), with permission from the American Society for Microbiology.

Citation: Mascaretti O. 2003. Structure and Function of Prokaryotic and Eukaryotic Cells, p 1-32. In Bacteria versus Antibacterial Agents. ASM Press, Washington, DC. doi: 10.1128/9781555817794.ch1
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Image of Figure 1.2
Figure 1.2

Fluid mosaic model of the cytoplasmic membrane structure. Reprinted from G. M. Cooper, The Cell: a Molecular Approach (ASM Press, Washington, D.C., and Sinauer Associates, Inc., Sunderland, Mass., 2000), with permission from the American Society for Microbiology.

Citation: Mascaretti O. 2003. Structure and Function of Prokaryotic and Eukaryotic Cells, p 1-32. In Bacteria versus Antibacterial Agents. ASM Press, Washington, DC. doi: 10.1128/9781555817794.ch1
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Image of Figure 1.3
Figure 1.3

Schematic three-dimensional model and comparison of eukaryotic and prokaryotic ribosomes.

Citation: Mascaretti O. 2003. Structure and Function of Prokaryotic and Eukaryotic Cells, p 1-32. In Bacteria versus Antibacterial Agents. ASM Press, Washington, DC. doi: 10.1128/9781555817794.ch1
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Image of Figure 1.4
Figure 1.4

Structure of microtubules. Dimers of α- and β-tubulin polymerize to form microtubules, which are composed of 13 protofilaments assembled around a hollow core. Reprinted from G. M. Cooper, The Cell: a Molecular Approach (ASM Press, Washington, D.C., and Sinauer Associates, Inc., Sunderland, Mass., 2000), with permission from the American Society for Microbiology.

Citation: Mascaretti O. 2003. Structure and Function of Prokaryotic and Eukaryotic Cells, p 1-32. In Bacteria versus Antibacterial Agents. ASM Press, Washington, DC. doi: 10.1128/9781555817794.ch1
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Image of Figure 1.5
Figure 1.5

Morphologies of some commonly encountered bacteria. Reprinted from T. S. Walker, Microbiology (The W. B. Saunders Co., Philadelphia, Pa., 1998), with permission from the publisher.

Citation: Mascaretti O. 2003. Structure and Function of Prokaryotic and Eukaryotic Cells, p 1-32. In Bacteria versus Antibacterial Agents. ASM Press, Washington, DC. doi: 10.1128/9781555817794.ch1
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Image of Figure 1.6
Figure 1.6

Diagrammatic representation of a gram-negative bacterial cell.

Citation: Mascaretti O. 2003. Structure and Function of Prokaryotic and Eukaryotic Cells, p 1-32. In Bacteria versus Antibacterial Agents. ASM Press, Washington, DC. doi: 10.1128/9781555817794.ch1
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Image of Figure 1.7
Figure 1.7

Schematic representation of the major surface structures of the cell wall of gram-positive bacteria. Abbreviations: TA, teichoic acid; LTA, lipoteichoic acid. Reprinted from V. A. Fischetti, R. P. Novick, J. F. Ferretti, D. A. Portnoy, and J. L. Rood (ed.), Gram- Positive Pathogens (ASM Press, Washington, D.C., 2000), with permission from the American Society for Microbiology.

Citation: Mascaretti O. 2003. Structure and Function of Prokaryotic and Eukaryotic Cells, p 1-32. In Bacteria versus Antibacterial Agents. ASM Press, Washington, DC. doi: 10.1128/9781555817794.ch1
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Image of Figure 1.8
Figure 1.8

Schematic representation of the major surface structures of the cell wall of gram-negative bacteria. Reprinted from L. E. Bryan (ed.), Antimicrobial Drug Resistance (Academic Press, Inc., San Diego, Calif., 1984), with permission from the publisher.

Citation: Mascaretti O. 2003. Structure and Function of Prokaryotic and Eukaryotic Cells, p 1-32. In Bacteria versus Antibacterial Agents. ASM Press, Washington, DC. doi: 10.1128/9781555817794.ch1
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Image of Figure 1.9
Figure 1.9

Structure of one of the repeating units of the peptidoglycan cell wall structure, the glycan tetrapeptide. Each monosaccharide derivative (G) is attached to other monosaccharide derivatives (M) by β1→4 glycosidic bonds. The structure illustrated is that found in E. coli and most other gram-negative bacteria. In some bacteria, other amino acids are found.

Citation: Mascaretti O. 2003. Structure and Function of Prokaryotic and Eukaryotic Cells, p 1-32. In Bacteria versus Antibacterial Agents. ASM Press, Washington, DC. doi: 10.1128/9781555817794.ch1
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Image of Figure 1.10
Figure 1.10

Peptidoglycan cross-links. (a) E. coli peptidoglycan; (b) S. aureus peptidoglycan. The abbreviations and structures of amino acid in the figure are given in appendix A.

Citation: Mascaretti O. 2003. Structure and Function of Prokaryotic and Eukaryotic Cells, p 1-32. In Bacteria versus Antibacterial Agents. ASM Press, Washington, DC. doi: 10.1128/9781555817794.ch1
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Image of Figure 1.11
Figure 1.11

Diagrammatic representation of peptidoglycan structures with adjacent glycan strains cross-linked directly from the carboxyl-terminal <sc>D</sc>-alanine to the Ɛ-amino group of an adjacent tetrapeptide or through a peptide interbridge.

Citation: Mascaretti O. 2003. Structure and Function of Prokaryotic and Eukaryotic Cells, p 1-32. In Bacteria versus Antibacterial Agents. ASM Press, Washington, DC. doi: 10.1128/9781555817794.ch1
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Image of Figure 1.12
Figure 1.12

Reactions involved in the biosynthesis of UDP-MurNAc acid in S. aureus. Pi, inorganic phosphate.

Citation: Mascaretti O. 2003. Structure and Function of Prokaryotic and Eukaryotic Cells, p 1-32. In Bacteria versus Antibacterial Agents. ASM Press, Washington, DC. doi: 10.1128/9781555817794.ch1
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Image of Figure 1.13
Figure 1.13

Later stage of the reactions shown in Fig. 1.12. The reactions involved in the biosynthesis of UDP-MurNAc pentapeptide (first stage) in S. aureus are shown.

Citation: Mascaretti O. 2003. Structure and Function of Prokaryotic and Eukaryotic Cells, p 1-32. In Bacteria versus Antibacterial Agents. ASM Press, Washington, DC. doi: 10.1128/9781555817794.ch1
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Image of Figure 1.14
Figure 1.14

Later stage of the reaction shown in Fig. 1.13. The reactions involved in the biosynthesis of linear chain of peptidoglycan units in S. aureus are shown.

Citation: Mascaretti O. 2003. Structure and Function of Prokaryotic and Eukaryotic Cells, p 1-32. In Bacteria versus Antibacterial Agents. ASM Press, Washington, DC. doi: 10.1128/9781555817794.ch1
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Image of Figure 1.15
Figure 1.15

Final stage of the biosynthesis of peptidoglycan in S. aureus.

Citation: Mascaretti O. 2003. Structure and Function of Prokaryotic and Eukaryotic Cells, p 1-32. In Bacteria versus Antibacterial Agents. ASM Press, Washington, DC. doi: 10.1128/9781555817794.ch1
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Image of Figure 1.16
Figure 1.16

General structures of some tei- (b) choic acids. (a) Ribitol teichoic acid. R =ββ-glucosyl residues in B. subtilis and α- or β-linked N-acetylglucosamine in various strains of S. aureus. (b) Glycerol teichoic acid. R = α-glucosyl residues in B. subtilis.

Citation: Mascaretti O. 2003. Structure and Function of Prokaryotic and Eukaryotic Cells, p 1-32. In Bacteria versus Antibacterial Agents. ASM Press, Washington, DC. doi: 10.1128/9781555817794.ch1
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Image of Figure 1.17
Figure 1.17

Generalized structure of the teichuronic acid present in the wall of B. licheniformis.

Citation: Mascaretti O. 2003. Structure and Function of Prokaryotic and Eukaryotic Cells, p 1-32. In Bacteria versus Antibacterial Agents. ASM Press, Washington, DC. doi: 10.1128/9781555817794.ch1
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Image of Figure 1.18
Figure 1.18

Molecular representation of the envelope of a gram-negative bacterium. Ovals and rectangles represent sugar residues, whereas circles depict polar head groups of the glycerophospholipids (phosphatidylethanolamine and phosphatidylglycerol). KDO and MDO represent membrane-derived oligosaccharides. The core region shown is that of E. coli K-12, a strain that does not normally contain an O-antigen repeat unless transformed with an appropiate plasmid. Reprinted from C. R. H. Raetz, J. Bacteriol. 175:5745–5753, 1993, with permission from the American Society for Microbiology.

Citation: Mascaretti O. 2003. Structure and Function of Prokaryotic and Eukaryotic Cells, p 1-32. In Bacteria versus Antibacterial Agents. ASM Press, Washington, DC. doi: 10.1128/9781555817794.ch1
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Image of Figure 1.19
Figure 1.19

Diagram showing the molecular structure of LPS in Salmonella species. LPS is composed of three major regions: the type-specific O antigen, which extends into the external environment from the bacterial surface; the core, which consists of inner and outer cores and which anchors the O antigen to the membrane; and lipid A, which is a phospholipid-like molecule that is embedded in the outer leaflet of the outer membrane.

Citation: Mascaretti O. 2003. Structure and Function of Prokaryotic and Eukaryotic Cells, p 1-32. In Bacteria versus Antibacterial Agents. ASM Press, Washington, DC. doi: 10.1128/9781555817794.ch1
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Image of Figure 1.20
Figure 1.20

Structure of S. enteric serovar Typhimurium LPS. The moleculeis made up of the side chain (Abe, abequose; Man, d-mannose; Rha, l-rhamnose; OAc, O-acetyl) linked to the core oligosaccharide (Gal, d-galactose; GlcNAc, N-acetylglucosamine; Glc, d-glucose; Hep, l-glycero-Dmannoheptose; EtN, ethanolamine) and lipid A (GlcN, d-glucosamine; AraN, 4-aminoarabinose). The fatty acid substituents are present in both amide and ester linkages.

Citation: Mascaretti O. 2003. Structure and Function of Prokaryotic and Eukaryotic Cells, p 1-32. In Bacteria versus Antibacterial Agents. ASM Press, Washington, DC. doi: 10.1128/9781555817794.ch1
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Image of Figure 1.21
Figure 1.21

Ribbon diagram of the OmpF porin from E. coli. (a) View from within the plane of the membrane onto the face of the barrel closest to the threefold axis. (b) View of the trimer looking along the threefold axis (triangle) from outside the cell. Reprinted from S. W. Cowan, Curr. Opin. Struct. Biol. 3:501–507, 1993, with permission from the publisher.

Citation: Mascaretti O. 2003. Structure and Function of Prokaryotic and Eukaryotic Cells, p 1-32. In Bacteria versus Antibacterial Agents. ASM Press, Washington, DC. doi: 10.1128/9781555817794.ch1
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Image of Figure 1.22
Figure 1.22

Chemical structures of cholesterol (a steroid) and diploptene (a hopanoid).

Citation: Mascaretti O. 2003. Structure and Function of Prokaryotic and Eukaryotic Cells, p 1-32. In Bacteria versus Antibacterial Agents. ASM Press, Washington, DC. doi: 10.1128/9781555817794.ch1
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Image of Figure 1.23
Figure 1.23

(Left) Fundamental structure of a phospholipid bilayer. (Right) Structures of a polar membrane phospholipid, phosphatidylethanolamine, which forms the hydrophilic region, and fatty acids (long chains), which are esterified to glycerol in the hydrophobic region.

Citation: Mascaretti O. 2003. Structure and Function of Prokaryotic and Eukaryotic Cells, p 1-32. In Bacteria versus Antibacterial Agents. ASM Press, Washington, DC. doi: 10.1128/9781555817794.ch1
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Image of Figure 1.24
Figure 1.24

Morphology of a gram-positive bacterium showing the mesosome, as well as other structures.

Citation: Mascaretti O. 2003. Structure and Function of Prokaryotic and Eukaryotic Cells, p 1-32. In Bacteria versus Antibacterial Agents. ASM Press, Washington, DC. doi: 10.1128/9781555817794.ch1
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Image of Figure 1.25
Figure 1.25

Ultrastructure of bacterial flagella. Flagellar basal bodies, hook, and filament in gram-negative (a) and gram-positive (b) bacteria are shown. Reprinted from L. M. Prescott, J. P. Harley, and D. A. Klein, Microbiology, 4th ed. (McGraw-Hill, Boston, Mass., 1999), with permission from the publisher.

Citation: Mascaretti O. 2003. Structure and Function of Prokaryotic and Eukaryotic Cells, p 1-32. In Bacteria versus Antibacterial Agents. ASM Press, Washington, DC. doi: 10.1128/9781555817794.ch1
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Image of Figure 1.26
Figure 1.26

Photomicrograph of two E. coli cells shows a bacterial mating (conjugation) process. The cell at the left has several common pili and a sex pilus connected to the right cell. The cell at the right lacks common pili. Reprinted from T. S. Walker, Microbiology (The W. B. Saunders Co., Philadelphia, Pa., 1998), with permission from the publisher.

Citation: Mascaretti O. 2003. Structure and Function of Prokaryotic and Eukaryotic Cells, p 1-32. In Bacteria versus Antibacterial Agents. ASM Press, Washington, DC. doi: 10.1128/9781555817794.ch1
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Image of Figure 1.27
Figure 1.27

The bacterial chromosome and supercoiling. (a) The DNA double helix in the shape of a closed circle. (b) Supercoiled form of circular DNA.

Citation: Mascaretti O. 2003. Structure and Function of Prokaryotic and Eukaryotic Cells, p 1-32. In Bacteria versus Antibacterial Agents. ASM Press, Washington, DC. doi: 10.1128/9781555817794.ch1
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Image of Figure 1.28
Figure 1.28

Diagrammatic representation of the strucure of the B form of DNA. The model shows the complementarity of the bases A-T and C-G and the antiparallel orientation of the two strands of polynucleotides.

Citation: Mascaretti O. 2003. Structure and Function of Prokaryotic and Eukaryotic Cells, p 1-32. In Bacteria versus Antibacterial Agents. ASM Press, Washington, DC. doi: 10.1128/9781555817794.ch1
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Image of Figure 1.29
Figure 1.29

Diagrammatic representation of semiconservative DNA replication. The replication fork of DNA and the synthesis of two progeny strands are shown. Each copy contains one new and one old strand.

Citation: Mascaretti O. 2003. Structure and Function of Prokaryotic and Eukaryotic Cells, p 1-32. In Bacteria versus Antibacterial Agents. ASM Press, Washington, DC. doi: 10.1128/9781555817794.ch1
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Image of Figure 1.30
Figure 1.30

Cloverleaf secondary structure of tRNA. Watson-Crick base pairing is indicated by dashed lines between nucleotide residues. The molecule is divided into an acceptor stem and four arms. Reprinted from L. M. Prescott, J. P. Harley, and D. A. Klein, Microbiology, 4th ed. (McGraw-Hill, Boston, Mass., 1999), with permission from the publisher.

Citation: Mascaretti O. 2003. Structure and Function of Prokaryotic and Eukaryotic Cells, p 1-32. In Bacteria versus Antibacterial Agents. ASM Press, Washington, DC. doi: 10.1128/9781555817794.ch1
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References

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1. Brooks, G. F.,, J. S. Butel,, and S. A. Morse. 1998. Jawetz, Melnick, & Adelberg's Medical Microbiology, 21st ed. Appleton & Lange, Stamford, Conn.
2. Cooper, G. M. 2000. The Cell: A Molecular Approach, 2nd ed. ASM Press, Washington, D.C., and Sinauer Associates, Inc., Sunderland, Mass.
3. Fischetti, V. A.,, R. P. Novick,, J. J. Ferretti,, D. A. Portnoy,, and J. I. Rood (ed.). 2000. Gram-Positive Pathogens. ASM Press, Washington, D.C.
4. Lengeler, J. W.,, G. Drews,, and H. G. Schlegel. 1999. Biology of the Prokaryotes. Georg Thieme Verlag, Stuttgart, Germany.
5. Madigan, M. T.,, J. M. Martinko,, and J. Parker. 2000. Brock Biology of Microorganisms , 9th ed. Prentice-Hall, Upper Saddle River, N.J.
6. Nelson, D. L.,, and M. M. Cox. 2000. Lehninger Principles of Biochemistry, 3rd ed. Worth Publishers, New York, N.Y.
7. Prescott, L. M.,, J. P. Harley,, and D. A. Klein. 1999. Microbiology , 4th ed. McGraw-Hill, Boston, Mass.
8. Salyers, A. A.,, and D. D. Whitt. 2001. Microbiology. Fitzgerald Science Press, Bethesda, Md.
9. Walker, T. S. 1998. Microbiology. The W. B. Saunders Co., Philadelphia, Pa.
10. White, D. 2000. The Physiology and Biochemistry of Prokaryotes. Oxford University Press, New York, N.Y.
11. Beveridge, T. J. Bacterial cell wall. Accepted for publication in Encyclopedia of Life Sciences. Nature Publishing, London, United Kingdom.
12. Ghuysen, J. M.,, and R. Hakenbeck. 1994. Bacterial Cell Wall . Elsevier, Amsterdam, The Netherlands.
13. Volker-Höltje, J., 2000. Cell walls, bacterial, p. 759771. In J. Lederberg (ed.), Encyclopedia of Microbiology , 2nd ed., vol. 1. Academic Press, Inc., San Diego, Calif.
14. Ward, J. B., 1990. Cell wall structure and function, p. 553607. In C. Hansch,, P. G. Sammes,, and J. B. Taylor (ed.), Comprehensive Medicinal Chemistry , vol. 2. Pergamon Press, Oxford, United Kingdom.
15. Benson, T. E.,, D. B. Prince,, V. T. Mutchler,, K. A. Curry,, A. M. Ho,, R. W. Sarver,, J. C. Hagadorn,, G. H. Choi,, and R. L. Garlick. 2002. X-ray crystal structure of Staphylococcus aureus FemA. Structure 10:11071115.
16. van Heijenoort, J. 2001. Recent advances in the formation of the bacterial peptidoglycan monomer unit. Nat. Prod. Rep. 18:503519.
17. Li, X.,, and H. L. T. Mobley. Bacterial pili and fimbriae. Accepted for publication in Encyclopedia of Life Sciences. Nature Publishing, London, United Kingdom.
18. Mulvey, M. A.,, K. W. Dodson,, G. E. Soto,, and S. J. Hultgren., 2000. Fimbriae, pili, p. 361379. In J. Lederberg (ed.), Encyclopedia of Microbiology , 2nd ed., vol. 2. Academic Press, Inc., San Diego, Calif.
19. Aizawa, S. I., 2000. Flagella, p. 380389. In J. Lederberg (ed.), Encyclopedia of Microbiology , 2nd ed., vol. 2, Academic Press, Inc., San Diego, Calif.
20. Manson, M. D.,, J. P. Armitage,, J. A. Hoch,, and R. M. Macnab. 1998. Bacterial locomotion and signal transduction. J. Bacteriol. 180:10091022.
21. Morgan, D. G.,, and S. Khan. Bacterial flagella. Accepted for publication in Encyclopedia of Life Sciences. Nature Publishing, London, United Kingdom.
22. Fleischmann, R. D.,, M. D. Adams,, O. White,, R. A. Clayton,, E. F. Kirkness,, A. R. Kerlavage,, C. J. Bult,, J. F. Tomb,, B. A. Dougherty,, J. M. Merrick,, K. McKenney,, G. Sutton,, W. FitzHugh,, C. Fields,, J. D. Gocayne,, J. Scott,, R. Shirley,, L.-I. Liu,, A. Glodek,, J. M. Kelley,, J. F. Weidman,, C. A. Phillips,, T. Spriggs,, E. Hedblom,, M. D. Cotton,, T. Utterback,, M. C. Hanna,, D. T. Nguyen,, D. M. Saudek,, R. C. Brandon,, L. D. Fine,, J. L. Fritchman,, J. L. Fuhrmann,, N. S. M. Geoghagen,, C. L. Gnehm,, L. A. McDonald,, K. V. Small,, C. M. Fraser,, H. O. Smith,, and J. C. Venter. 1995. Whole-genome random sequencing and assembly of Haemophilus influenzae. Science 269:496512.
23. Guild, B. C. 1999. Genomics, target selection, validation, and assay considerations in the development of antibacterial screens. Annu. Rep. Med. Chem. 34:227239.
24. Heidelberg, J. F.,, J. A. Eisen,, W. C. Nelson,, R. A. Clayton,, M. L. Gwinn,, R. J. Dodson,, D. H. Haft,, E. K. Hickey,, J. D. Peterson,, L. Umayan,, S. R. Gill,, K. E. Nelson,, T. D. Read,, H. Tettelin,, D. Richardson,, M. D. Ermolaeva,, J. Vamathevan,, S. Bass,, H. Qin,, I. Dragoi,, P. Sellers,, L. McDonald,, T. Utterback,, R. D. Fleishmann,, W. C. Nierman,, O. White,, S. L. Salzberg,, H. O. Smith,, R. R. Colwell,, J. J. Mekalanos,, J. C. Venter,, and C. M. Fraser. 2000. DNA sequence of both chromosomes of the cholera pathogen Vibrio cholerae. Nature 406:477483.
25. Jenks, P. J. 1998. Sequencing microbial genomes—what will it do for microbiology? J. Med. Microbiol. 47:375382.
26. Kuroda, M.,, T. Ohta,, I. Uchiyama,, T. Baha,, H. Yuzawa,, I. Kobayashi,, L. Cui,, A. Oguchi,, K. Acki,, Y. Nagai,, J. Lian,, T. Ito,, M. Kanamori,, H. Matsumaru,, A. Maruyama,, H. Murakami,, A. Hosoyama,, Y. Mizutani-Ui,, N. K. Takahashi,, T. Sawano,, R. Inoue,, C. Kaito,, K. Sekimizu,, H. Hirakawa,, S. Kuhara,, S. Goto,, J. Yabuzaki,, M. Kanehisa,, A. Yamashita,, K. Oshima,, K. Furuya,, C. Yoshino,, T. Shiba,, M. Hattori,, N. Ogasawara,, H. Hayashi,, and K. Hiramatsu. 2001. Whole genome sequencing of methicillin-resistant Staphylococcus aureus. Lancet 357:12251240.
27. Moir, D. T.,, K. J. Shaw,, R. S. Hare,, and G. F. Vovis. 1999. Genomics and antimicrobial drug discovery. Antimicrob. Agents Chemother. 43:439446.
28. Stover, C. K.,, X. Q. Pham,, A. L. Erwin,, S. D. Mizoguchi,, P. Warrener,, M. J. Hickey,, F. S. L. Brinkman,, W. O. Hufnagle,, D. J. Kowalik,, M. Lagrou,, R. L. Garber,, L. Goltry,, E. Tolentino,, S. Westbrock-Wadman,, Y. Yuan,, L. L. Brody,, S. N. Coulter,, K. R. Folger,, A. Kas,, K. Larbig,, R. Lim,, K. Smith,, D. Spencer,, G. K. S. Wong,, Z. Wu,, I. T. Paulsen,, J. Reizer,, M. H. Saier,, R. E. W. Hancock,, S. Lory,, and M. V. Olson. 2000. Complete genome sequence of Pseudomonas aeruginosa PA01, an opportunistic pathogen. Nature 406:959964.
29. Strauss, E. J.,, and S. Falkow. 1997. Microbial pathogenesis: genomics and beyond. Science 276:707712.
30. Robinow, C.,, and E. Kellenberger. 1994. The bacterial nucleoid revisited. Microbiol. Rev. 58:211232.
31. Braun, V. 1975. Covalent lipoprotein from the outer membrane of Escherichia coli. Biochim. Biophys. Acta 415:335377.
32. Caroff, M.,, D. Karibian,, J. M. Cavaillon,, and N. Haefner-Cavaillon. 2002. Structural and functional analyses of bacterial lipopolysaccharides. Microbes Infect. 4:915926.
33. Hancock, R. E. W. 1991. Bacterial outer membranes: evolving concepts. ASM News 57:175182.
34. Koebnik, K. R.,, K. P. Locher,, and P. Van Gelden. 2000. Structure and function of bacterial outer membrane proteins: barrels in a nutshell. Mol. Microbiol. 37:239253.
35. Nikaido, H. 1989. Outer membrane barrier as a mechanism of antimicrobial resistance. Antimicrob. Agents Chemother. 33:18311836.
36. Nikaido, H.,, and M. Vaara. 1985. Molecular basis of bacterial outer membrane permeability. Microbiol. Rev. 49:132.
37. Noland, B. W.,, J. M. Newman,, J. Hendle,, J. Badger,, J. A. Christopher,, J. Tresser,, M. D. Buchanan,, T. A. Wright,, H. J. Müller-Dieckmann,, K. S. Gajiwala,, and S. G. Buchanan. 2002. Structural studies of Salmonella typhimurium ArnB (PmrH) aminotransferase: a 4-amino-4-deoxy-L-arabinose lipopolysaccharide- modifying enzyme. Structure 10:15691580.
38. Calamita, G. 2000. The Escherichia coli aquaporin-Z water channel. Mol. Microbiol. 37:254262.
39. Cowan, S. W. 1993. Bacterial porins: lessons from three highresolution structures. Curr. Opin. Struc. Biol. 3:501507.
40. Cowan, S. W.,, T. Schirmer,, G. Rummel,, M. Steiert,, R. Ghosh,, R. A. Pauptit,, J. N. Jansonius,, and J. P. Rosenbusch. 1992. Crystal structures explain functional properties of two E. coli porins. Nature 358:727733.
41. Doménech-Sánchez, A.,, S. Hernández-Allés,, L. Martínez- Martínez,, V. J. Benedí,, and S. Alberti. 1999. Identification and characterization of a new porin gene of Klebsiella pneumoniae: its role in β-lactam antibiotic resistance. J. Bacteriol. 181:27262732.
42. Hancock, R. E. W. 1987. Role of porins in outer membrane permeability. J. Bacteriol. 169:929933.
43. Misuno, T.,, M. Y. Chou,, and M. Inouye. 1983. A comparative study on the genes for three porins of the Escherichia coli outer membrane. J. Biol. Chem. 258:69326940.
44. Nikaido, H. 1992. Porins and specific channels of bacterial outer membranes. Mol. Microbiol. 6:435442.
45. Schirmer, T.,, T. A. Keller,, Y.-F. Wang,, and J. P. Rosenbusch. 1995. Structural basis for sugar translocation through maltoporin channels at 3.1 Å resolution. Science 267:512514.
46. Schirmer, T.,, and J. P. Rosenbusch. 1991. Proterozoic and eukaryotic porins. Curr. Biol. 1:539545.
47. Schulz, G. E., 1994. Structure-function relationships in porins as derived from a 1.8 Å resolution crystal structure, p. 343352. In J. M. Ghuysen, and R. Hakenbeck (ed.), Bacterial Cell Wall. Elsevier, Amsterdam, The Netherlands.
48. Schulz, G. E. 1993. Bacterial porins: structure and function. Curr. Biol. 3:701707.
49. Weis, M. S.,, and G. E. Schulz. 1992. Structure of porin refined at 1.8 Å resolution. J. Mol. Biol . 227:493509.
50. Ban, B.,, P. Nissen,, J. Hansen,, P. B. Moore,, and T. A. Steitz. 2000. The complete atomic structure of the large ribosomal subunit at 2.4 Å resolution. Science 289:905920.
51. Cate, J. H.,, M. M. Yusupov,, G. Z. Yusupova,, T. N. Earnest,, and H. F. Noller. 1999. X-ray crystal structures of 70S ribosome functional complexes. Science 285:20952104.
52. Clemons, W. M.,, J. L. C. May,, B. T. Wimberly,, J. P. McCutcheon,, M. S. Capel,, and V. Ramakrishnan. 1999. Structure of a bacterial 30S ribosomal subunit at 5.5 Å resolution. Nature 400:833847.
53. Garrett, R. 1999. Mechanics of the ribosome. Nature 400:811812.
54. Garrett, R. A.,, S. R. Douthwaite,, A. Liljas,, A. T. Matheson,, P. B. Moore,, and H. F. Nolle (ed.). 2000. The Ribosome: Structure, Function, Antibiotics, and Cellular Interactions. ASM Press, Washington, D.C.
55. Squires, C. L., 2000. Ribosome synthesis and regulation, p. 127139. In J. Lederberg (ed.), Encyclopedia of Microbiology , 2nd ed., vol. 4. Academic Press, Inc., San Diego, Calif.
56. Tocilj, A.,, F. Schlunzen,, D. Janell,, M. Gluhmann,, H. A. S. Hansen,, J. Harms,, A. Bashan,, H. Bartels,, I. Agmon,, F. Franceschi,, and A. Yonath. 1999. The small ribosomal subunit from Thermus thermophilus at 4.5 Å resolution: Patter fittings and identification of a functional site. Proc. Natl. Acad. Sci. USA 96:1425214257.
57. Westhof, E.,, and N. Leontis. 2000. Atomic glimpses on a billion-year old molecular machine. Angew. Chem. Int. Ed. English 39:15871591.
58. Yusupov, M. M.,, G. Z. Yusupova,, A. Baucom,, K. Lieberman,, T. N. Earnest,, J. H. D. Cate,, and H. F. Noller. 2001. Crystal structure of the ribosome at 5.5 Å resolution. Science 292:883902.
59. Soll, D.,, and U. L. RajBhandary (ed.). 1995. tRNA: Structure, Biosynthesis, and Function. ASM Press, Washington, D.C.
60. DeHaseth, P. L.,, M. L. Zupancic,, and M. T. Record. 1998. RNA polymerase-promoter interactions: the coming and goings of RNA polymerase. J. Bacteriol. 180:30193025.

Tables

Generic image for table
Table 1.1

Comparison of prokaryotic and eukaryotic cell organization a

Citation: Mascaretti O. 2003. Structure and Function of Prokaryotic and Eukaryotic Cells, p 1-32. In Bacteria versus Antibacterial Agents. ASM Press, Washington, DC. doi: 10.1128/9781555817794.ch1
Generic image for table
Table 1.2

Functions of animal eukaryotic organelles a

Citation: Mascaretti O. 2003. Structure and Function of Prokaryotic and Eukaryotic Cells, p 1-32. In Bacteria versus Antibacterial Agents. ASM Press, Washington, DC. doi: 10.1128/9781555817794.ch1
Generic image for table
Table 1.3

Functions of prokaryotic structures a

Citation: Mascaretti O. 2003. Structure and Function of Prokaryotic and Eukaryotic Cells, p 1-32. In Bacteria versus Antibacterial Agents. ASM Press, Washington, DC. doi: 10.1128/9781555817794.ch1

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