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Internal presequences

The above describes the major pathway of proteins destined for the mitochondrial matrix. However, certain proteins insert into the outer mitochoiidrial membrane facilitated by the TOM complex. Others stop in the intermembrane space, and some insert into the inner membrane. Yet others proceed into the matrix and then return to the inner membrane or intermembrane space. A number of proteins contain two signaling sequences—one to enter the mitochondrial matrix and the other to mediate subsequent relocation (eg, into the inner membrane). Certain mitochondrial proteins do not contain presequences (eg, cytochrome Cy which locates in the inter membrane space), and others contain internal presequences. Overall, proteins employ a variety of mechanisms and routes to attain their final destinations in mitochondria. [Pg.501]

This a-helix is amphipathic, containing patches of positively charged and hydrophobic amino acids, respectively, on opposite surfaces of the theoretical cylinder. The presequence is usually processed by the mitochondrial processing peptidase (MPP) and the mature protein is sorted to either the matrix, or to the inner membrane if it bears a hydrophobic stop-transfer sequence. Some mitochondrial proteins, mostly destined to the membranes, do not have cleavable N-terminal presequences but have internal targeting signals that are not well characterized (Pfanner and Geissler 2001). [Pg.25]

Mitochondria arise by division and growth of preexisting mitochondria. Because they synthesize only a few proteins and RNA molecules, they must import many proteins and other materials from the cytoplasm. A mitochondrion contains at least 100 proteins that are encoded by nuclear genes.50,50a The mechanisms by which proteins are taken up by mitochondria are complex and varied. Many of the newly synthesized proteins carry, at the N terminus, presequences that contain mitochondrial targeting signals51-53 (Chapter 10). These amino acid sequences often lead the protein to associate with receptor proteins on the outer mitochondrial membrane and subsequently to be taken up by the mitochondria. While the targeting sequences are usually at the N terminus of a polypeptide, they are quite often internal. The N-terminal sequences are usually removed by action of the mitochondrial processing peptidase (MPP) in... [Pg.1018]

Current evidence suggests that luminal mitosomal proteins can be imported into the organelle via two clearly distinct routes one that requires the presence of amino-terminal targeting presequences equivalent to those present in mitochondrial and hydrogenosomal proteins and an alternative presequence-independent pathway that seems to rely on the recognition of internal targeting sequences (Bradley et al. 1997 Wiedemann et al. 2004). The experimental evidence for the existence of each of these pathways is discussed next. [Pg.287]


See other pages where Internal presequences is mentioned: [Pg.312]    [Pg.314]    [Pg.25]    [Pg.30]    [Pg.35]    [Pg.43]    [Pg.45]    [Pg.47]    [Pg.51]    [Pg.210]    [Pg.211]    [Pg.182]    [Pg.258]    [Pg.289]    [Pg.105]    [Pg.8]    [Pg.6]   
See also in sourсe #XX -- [ Pg.501 ]




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Presequence

Presequences

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