Integration of the mitochondrial-processing peptidase into the cytochrome bc1 complex in plants
- PMID: 10591532
- DOI: 10.1023/a:1005475930477
Integration of the mitochondrial-processing peptidase into the cytochrome bc1 complex in plants
Abstract
The plant mitochondrial cytochrome bc1 complex, like nonplant mitochondrial complexes, consists of cytochromes b and c1, the Rieske iron-sulfur protein, two Core proteins, and five low-molecular mass subunits. However, in contrast to nonplant sources, the two Core proteins are identical to subunits of the general mitochondrial processing peptidase (MPP). The MPP is a fascinating enzyme that catalyzes the specific cleavage of the diverse presequence peptides from hundreds of the nuclear-encoded mitochondrial precursor proteins that are synthesized in the cytosol and imported into the mitochondrion. Integration of the MPP into the bc1 complex renders the bc1 complex in plants bifunctional, being involved both in electron transport and in protein processing. Despite the integration of MPP into the bc1 complex, electron transfer as well as translocation of the precursor through the import channel are independent of the protein-processing activity. Recognition of the processing site by MPP occurs via the recognition of higher-order structural elements in combination with charge and cleavage-site properties. Elucidation of the three-dimensional (3-D) structure of the mammalian cytochrome bc1 complex is highly useful for understanding of the mechanism of action of MPP.
Similar articles
-
Bifunctional role of the bc1 complex in plants. Mitochondrial bc1 complex catalyses both electron transport and protein processing.FEBS Lett. 1994 Jun 6;346(1):83-7. doi: 10.1016/0014-5793(94)00312-2. FEBS Lett. 1994. PMID: 8206164 Review.
-
Studies on the topology of the protein import channel in relation to the plant mitochondrial processing peptidase integrated into the cytochrome bc1 complex.Plant J. 2000 Dec;24(5):637-44. doi: 10.1046/j.1365-313x.2000.00910.x. Plant J. 2000. PMID: 11123802
-
Studies on protein processing for membrane-bound spinach leaf mitochondrial processing peptidase integrated into the cytochrome bc1 complex and the soluble rat liver matrix mitochondrial processing peptidase.Eur J Biochem. 1996 Nov 15;242(1):114-21. doi: 10.1111/j.1432-1033.1996.0114r.x. Eur J Biochem. 1996. PMID: 8954161
-
Activation of a matrix processing peptidase from the crystalline cytochrome bc1 complex of bovine heart mitochondria.J Biol Chem. 1998 Aug 14;273(33):20752-7. doi: 10.1074/jbc.273.33.20752. J Biol Chem. 1998. PMID: 9694818
-
The mitochondrial processing peptidase: function and specificity.Experientia. 1996 Dec 15;52(12):1077-82. doi: 10.1007/BF01952105. Experientia. 1996. PMID: 8988249 Review.
Cited by
-
Mitochondrial biogenesis and function in Arabidopsis.Arabidopsis Book. 2008;6:e0111. doi: 10.1199/tab.0111. Epub 2008 Jul 9. Arabidopsis Book. 2008. PMID: 22303236 Free PMC article.
-
The closed structure of presequence protease PreP forms a unique 10,000 Angstroms3 chamber for proteolysis.EMBO J. 2006 May 3;25(9):1977-86. doi: 10.1038/sj.emboj.7601080. Epub 2006 Apr 6. EMBO J. 2006. PMID: 16601675 Free PMC article.
-
An in silico analysis of the mitochondrial protein import apparatus of plants.BMC Plant Biol. 2010 Nov 16;10:249. doi: 10.1186/1471-2229-10-249. BMC Plant Biol. 2010. PMID: 21078193 Free PMC article.
-
Genome barriers between nuclei and mitochondria exemplified by cytoplasmic male sterility.Plant Cell Physiol. 2008 Oct;49(10):1484-94. doi: 10.1093/pcp/pcn102. Epub 2008 Jul 14. Plant Cell Physiol. 2008. PMID: 18625609 Free PMC article. Review.
-
The Plastid and Mitochondrial Peptidase Network in Arabidopsis thaliana: A Foundation for Testing Genetic Interactions and Functions in Organellar Proteostasis.Plant Cell. 2017 Nov;29(11):2687-2710. doi: 10.1105/tpc.17.00481. Epub 2017 Sep 25. Plant Cell. 2017. PMID: 28947489 Free PMC article. Review.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources