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Chapter 27 : Glutamyl-tRNA as an Intermediate in Glutamate Conversions

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Glutamyl-tRNA as an Intermediate in Glutamate Conversions, Page 1 of 2

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Abstract:

Since the discovery of initiator tRNA, a number of reactions have been found that involve modification of amino acids attached to tRNA. These reactions include well-understood processes like the formation of formylmethionyl-tRNA, which serves to initiate peptide chain formation in prokaryotes, or the synthesis of selenocysteine, which functions as the 21st amino acid. Less well understood are the conversions of glutamate. The first conversion serves for the formation of glutamate-1-semialdehyde, the initial precursor of porphyrins (e.g., chlorophylls and hemes). The other known reaction is a transamidation of glutamate attached to tRNA, which is a required intermediate in the formation of glutaminyl-tRNA in many organisms and organelles. These conversions of glutamate based on Glu-tRNA as intermediate are the topic of this chapter. Tetrapyrrole-containing compounds, such as hemes and chlorophylls, are essential components of respiratory and photosynthetic reactions. The porphyrin ring of these compounds is derived from eight molecules of 5-aminolevulinic acid (ALA), a precursor whose formation provides a key regulatory control point in heme and chlorophyll biosynthesis.

Citation: Verkamp E, Kumar A, Lloyd A, Martins O, Stange-Thomann N, Söll D. 1995. Glutamyl-tRNA as an Intermediate in Glutamate Conversions, p 545-550. In tRNA. ASM Press, Washington, DC. doi: 10.1128/9781555818333.ch27

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Figures

Image of Figure 1
Figure 1

The C5-pathway of ALA formation. Glu-tRNA reductase reduces Glu-tRNA to glutamate 1-semialdehyde, with the release of free tRNA. GSA is converted to ALA by glutamate 1- semialdehyde-2,l-aminomutase. The gene designations (for plant) and cofactor requirements are listed.

Citation: Verkamp E, Kumar A, Lloyd A, Martins O, Stange-Thomann N, Söll D. 1995. Glutamyl-tRNA as an Intermediate in Glutamate Conversions, p 545-550. In tRNA. ASM Press, Washington, DC. doi: 10.1128/9781555818333.ch27
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Image of Figure 2
Figure 2

Comparison of tRNA sequences. The sequence of barley chloroplast tRNA is shown. Nucleotides in circled positions (variable positions) designate differences in primary structure among the chloroplast and sp. PCC 6803 tRNA gene sequences compiled in Table 1 . Arrows indicate the differences (in addition to those found in the variable positions) between and barley chloroplast tRNA.

Citation: Verkamp E, Kumar A, Lloyd A, Martins O, Stange-Thomann N, Söll D. 1995. Glutamyl-tRNA as an Intermediate in Glutamate Conversions, p 545-550. In tRNA. ASM Press, Washington, DC. doi: 10.1128/9781555818333.ch27
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Image of Figure 3
Figure 3

The transamidation pathway of Gln-tRNA formation.

Citation: Verkamp E, Kumar A, Lloyd A, Martins O, Stange-Thomann N, Söll D. 1995. Glutamyl-tRNA as an Intermediate in Glutamate Conversions, p 545-550. In tRNA. ASM Press, Washington, DC. doi: 10.1128/9781555818333.ch27
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References

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Tables

Generic image for table
Table 1

Sequence alignment of chloroplast and Synechocystic 6803 tRNA genes

All sequences listed for comparison were obtained from GenBank or the EMBL data library. The organisms, with corresponding accession numbers, are as follows: (XO6378), (X15901), (X02805), (L20419), (X02217), (X00682), (X01676), (X04185), (X61798), (L20418), (L20417), (M20950), (J01412), (M22563), (X54406), and sp. PCC 6803 (M32099). The secondary structure features of the tRNA are indicated.

Citation: Verkamp E, Kumar A, Lloyd A, Martins O, Stange-Thomann N, Söll D. 1995. Glutamyl-tRNA as an Intermediate in Glutamate Conversions, p 545-550. In tRNA. ASM Press, Washington, DC. doi: 10.1128/9781555818333.ch27

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