Chapter 13 : Mitochondria and Respiration

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This chapter covers the functions of mitochondria in filamentous fungi. Mitochondrial respiration occurs via transfer of electrons from reduced electron carriers to molecular oxygen. This is accomplished using an electron transport chain housed in the mitochondrial inner membrane (MIM). Fungal mitochondrial genomes are AT-rich DNAs that map as circular molecules. However, several studies suggest that fungal mtDNAs are actually long, concatenated linear molecules. The study of fungal mitochondrial introns has been an active area of research that has yielded a number of significant findings. There are numerous reports of RNA elements being associated with mitochondria. Though they are formally classified as mitoviruses, they can also be considered plasmids based on their structural similarities to linear mt plasmids and lack of an extracellular form. The large number of different proteins that are found in mitochondria (probably about 1,000 for fungi) and the limited coding capacity of mtDNA emphasize the fact that most mitochondrial proteins are encoded by nuclear genes, translated in the cytosol, and imported into the organelle. The chapter attempts to define the basic import process and summarizes the literature while pointing out contributions that have involved filamentous fungi-almost entirely . Filamentous fungi are generally considered immortal. is an exception to this rule, as it has a defined vegetative- growth life span.

Citation: Nargang F, Kennell J. 2010. Mitochondria and Respiration, p 155-178. In Borkovich K, Ebbole D (ed), Cellular and Molecular Biology of Filamentous Fungi. ASM Press, Washington, DC. doi: 10.1128/9781555816636.ch13
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Image of FIGURE 1

Electron transport chain. Electrons from the reduced electron carriers NADH + Hand FADH are extracted by complex I and complex II, respectively, and transferred through the electron transport chain in the direction of the arrows. Complex IV uses the electrons to reduce molecular oxygen to water. The four large enzyme complexes are shown as black boxes. The pathway that ends at complex IV is referred to as the cytochrome-mediated electron transport chain (cmETC) in this chapter. At coenzyme Q (the ubiquinone/ubiquinol pool) the path to oxygen may branch in organisms capable of producing AOX. Complexes I, III, and IV are sites where electron transfer is coupled to proton pumping. The cmETC refers to the path of electrons from complex I to oxygen via complex IV since cytochromes and (found in complex III), cytochrome , and cytochromes and (found in complex IV) are involved in electron transfer via this path. Chemicals mentioned in the text that inhibit electron flow are shown in parentheses under the enzymes that they affect (Ant A, antimycin A; CN, cyanide; SHAM, salicylhydroxamic acid).

Citation: Nargang F, Kennell J. 2010. Mitochondria and Respiration, p 155-178. In Borkovich K, Ebbole D (ed), Cellular and Molecular Biology of Filamentous Fungi. ASM Press, Washington, DC. doi: 10.1128/9781555816636.ch13
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Image of FIGURE 2

Predicted placement of subunits in the peripheral or membrane arms of complex I ( ). The seven mitochondrially encoded subunits are referred to as NAD proteins but may be called ND proteins in some other references. The subunits encoded within the nucleus are referred to according to their molecular mass in kilodaltons.

Citation: Nargang F, Kennell J. 2010. Mitochondria and Respiration, p 155-178. In Borkovich K, Ebbole D (ed), Cellular and Molecular Biology of Filamentous Fungi. ASM Press, Washington, DC. doi: 10.1128/9781555816636.ch13
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Image of FIGURE 3

Complexes and proteins involved in import of proteins into mitochondria. Subunits of each complex are shown with a number representing their molecular mass. The TOM complex (translocase of the outer mitochondrial membrane) is the entry point for the majority of mitochondrial proteins. The SAM complex (sorting and assembly machinery) is also known as the TOB (topo-genesis of β-barrel proteins) complex (see Table 2 ). The SAM complex is responsible for the insertion of β-barrel proteins into the outer membrane following their import through the TOM complex into the IMS. Further assembly of β-barrel proteins requires the action of Mdm12 and Mmm1. Tom40 additionally requires the action of Mdm10 and Mim1. The two TIM complexes (translocases of the inner mitochondrial membrane) were named for the Tim22 and Tim23 proteins originally identified as components of the respective complex. Precursors of the carrier family (such as the ATP/ADP carrier) and a few other proteins with an even number of membrane-spanning domains and no cleavable presequence are inserted into the MIM by the TIM22 complex. Precursors with cleavable targeting signals are recognized as substrates by the TIM23 complex and translocated into the matrix. However, some TIM23 substrates contain stop-transfer signals that halt movement into the matrix and result in partitioning into the MIM. The PAM complex (presequence translocase associated motor) binds the N terminus of presequence-containing preproteins as they enter the matrix. Through cycles of interaction with mtHsp70, the precursor is drawn into the matrix. Two complexes composed of six small Tim protein subunits, either three subunits of Tim8 plus three of Tim13 or three of Tim9 plus three of Tim10, exist in the IMS. These complexes chaperone precursors en route to either the SAM complex or the TIM22 complex through the IMS. The OXA (cytochrome oxidase assembly) complex “exports” a small class of matrix targeted precursors back into the MIM from the matrix. It is also involved in the insertion of mitochondrial translation products into the MIM. The Mia40 and Erv1 proteins form a disulfide relay system that is responsible for trapping a class of small precursors with a twin cysteine motif into the IMS. Further details are given in the text.

Citation: Nargang F, Kennell J. 2010. Mitochondria and Respiration, p 155-178. In Borkovich K, Ebbole D (ed), Cellular and Molecular Biology of Filamentous Fungi. ASM Press, Washington, DC. doi: 10.1128/9781555816636.ch13
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Image of FIGURE 4

Electron tomographic image of the purified TOM core complex. The stain-filled pits are assumed to be pores through which preproteins cross the MOM. (From .)

Citation: Nargang F, Kennell J. 2010. Mitochondria and Respiration, p 155-178. In Borkovich K, Ebbole D (ed), Cellular and Molecular Biology of Filamentous Fungi. ASM Press, Washington, DC. doi: 10.1128/9781555816636.ch13
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Image of FIGURE 5

Steps in assembly of Tom40 into the TOM complex. Following synthesis in the cytosol, a Tom40 precursor is recognized by the TOM complex and imported into the IMS. The precursor then interacts with one of the small-Tim complexes that chaperone the precursor to the SAM complex. The precursor interacts with the SAM complex and forms assembly intermediate I. The SAM complex inserts the precursor into the membrane, where it associates with a preexisting Tom40 molecule and a molecule of Tom5 to give assembly intermediate II. Further assembly gives the fully formed TOM complex. The Mdm10, Mdm12, Mmm1, and Mim1 proteins are also required for efficient assembly of Tom40 at steps following interaction with the SAM complex.

Citation: Nargang F, Kennell J. 2010. Mitochondria and Respiration, p 155-178. In Borkovich K, Ebbole D (ed), Cellular and Molecular Biology of Filamentous Fungi. ASM Press, Washington, DC. doi: 10.1128/9781555816636.ch13
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