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Mam33p, an oligomeric, acidic protein in the mitochondrial matrix of Saccharomyces cerevisiae is related to the human complement receptor gC1q‐R
Author(s) -
Seytter Tilman,
Lottspeich Friedrich,
Neupert Walter,
Schwarz Elisabeth
Publication year - 1998
Publication title -
yeast
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.923
H-Index - 102
eISSN - 1097-0061
pISSN - 0749-503X
DOI - 10.1002/(sici)1097-0061(19980315)14:4<303::aid-yea217>3.0.co;2-n
Subject(s) - biology , intermembrane space , mitochondrial intermembrane space , saccharomyces cerevisiae , biochemistry , open reading frame , mitochondrion , mitochondrial matrix , signal peptide , protein targeting , hspa9 , peptide sequence , microbiology and biotechnology , gene , cytosol , bacterial outer membrane , membrane , enzyme , membrane protein , escherichia coli
Abstract Mam33p (mitochondrial acidic matrix protein) is a soluble protein, located in mitochondria of Saccharomyces cerevisiae . It is synthesized as a precursor with an N‐terminal mitochondrial targeting sequence that is processed on import. Mam33p assembles to a homo‐oligomeric complex in the mitochondrial matrix. It can bind to the sorting signal of cytochrome b 2 that directs this protein into the intermembrane space. Mam33p is encoded by an 801 bp open reading frame. Gene disruption did not result in a significant growth defect. Mam33p exhibits sequence similarity to gC1q‐R, a human protein that has been implicated in the binding of complement factor C1q and kininogen. © 1998 John Wiley & Sons, Ltd.