Article
Licensed
Unlicensed
Requires Authentication
Diverse mechanisms and machineries for import of mitochondrial proteins
-
Published/Copyright:
August 14, 2007
Abstract
Mitochondria are ubiquitous organelles that play an essential role in energy conversion and biosynthetic pathways in eukaryotic cells. Most mitochondrial proteins must be imported from the cytosol and sorted into one of the four mitochondrial subcompartments, the outer membrane, the intermembrane space, the inner membrane and the matrix. Studies in recent years revealed a remarkable diversity of mechanisms and machineries that are required for the import of proteins into mitochondria. At least four different pathways for the sorting and assembly of nuclear-encoded mitochondrial proteins have been identified.
Keywords: complex assembly; disulfide bonds; mitochondria; protein import; protein sorting; translocase
Published Online: 2007-08-14
Published in Print: 2007-09-01
©2007 by Walter de Gruyter Berlin New York
You are currently not able to access this content.
You are currently not able to access this content.
Articles in the same Issue
- To our authors, readers and subscribers ‘Just Accepted’ feature at http://www.atypon-link.com/WDG/loi/bchm
- Paper of the Year 2006: Award to Pamela Hamill
- The endosymbiotic origin of organelles: an ancient process still very much in fashion
- Solute channels of the outer membrane: from bacteria to chloroplasts
- Diverse mechanisms and machineries for import of mitochondrial proteins
- Transport of nuclear-encoded proteins into secondarily evolved plastids
- Mechanisms of protein import into thylakoids of chloroplasts
- Molecular machinery of mitochondrial dynamics in yeast
- Chloroplast photorelocation movement mediated by phototropin family proteins in green plants
- Plastid division in an evolutionary context
- Variability of the mitochondrial genome in mammals at the inter-species/intra-species boundary
- Diversity of proteasomal missions: fine tuning of the immune response
- Cellular expression of plasma prekallikrein in human tissues
- Sumoylation of the zinc finger protein ZXDC enhances the function of its transcriptional activation domain
- Josephin domain-containing proteins from a variety of species are active de-ubiquitination enzymes
- Cysteine protease inhibitors reduce brain β-amyloid and β-secretase activity in vivo and are potential Alzheimer's disease therapeutics
Keywords for this article
complex assembly;
disulfide bonds;
mitochondria;
protein import;
protein sorting;
translocase
Articles in the same Issue
- To our authors, readers and subscribers ‘Just Accepted’ feature at http://www.atypon-link.com/WDG/loi/bchm
- Paper of the Year 2006: Award to Pamela Hamill
- The endosymbiotic origin of organelles: an ancient process still very much in fashion
- Solute channels of the outer membrane: from bacteria to chloroplasts
- Diverse mechanisms and machineries for import of mitochondrial proteins
- Transport of nuclear-encoded proteins into secondarily evolved plastids
- Mechanisms of protein import into thylakoids of chloroplasts
- Molecular machinery of mitochondrial dynamics in yeast
- Chloroplast photorelocation movement mediated by phototropin family proteins in green plants
- Plastid division in an evolutionary context
- Variability of the mitochondrial genome in mammals at the inter-species/intra-species boundary
- Diversity of proteasomal missions: fine tuning of the immune response
- Cellular expression of plasma prekallikrein in human tissues
- Sumoylation of the zinc finger protein ZXDC enhances the function of its transcriptional activation domain
- Josephin domain-containing proteins from a variety of species are active de-ubiquitination enzymes
- Cysteine protease inhibitors reduce brain β-amyloid and β-secretase activity in vivo and are potential Alzheimer's disease therapeutics
