Difference between revisions of "Proteolysis"
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== Genes in this functional category == | == Genes in this functional category == | ||
| + | |||
| + | === Protein quality control === | ||
| + | * ''[[htrA]]'' | ||
| + | * ''[[htrB]]'' | ||
| + | * ''[[htrC]]'' | ||
| + | * ''[[wprA]]'' | ||
| + | |||
| + | === Extracellular feeding proteases === | ||
| + | * [[AprE]] and [[NprE]] account for 95% of extracellular proteolytic activity | ||
| + | |||
| + | * ''[[aprE]]'' | ||
* ''[[bpr]]'' | * ''[[bpr]]'' | ||
| + | * ''[[epr]]'' | ||
| + | * ''[[mpr]]'' | ||
| + | * ''[[nprB]]'' | ||
| + | * ''[[nprE]]'' | ||
| + | * ''[[vpr]]'' | ||
| + | |||
| + | * A mutant strain with deletions of all feeding proteases and the three major protein quality control proteases (''[[htrA]]'', ''[[htrB]]'', ''[[wprA]]'') (BRB14) is available in [[Colin Harwood]]'s lab {{PubMed|24115457}} | ||
| + | |||
| + | === Proteolysis during [[sporulation]]/ [[germination]] === | ||
| + | * ''[[gpr]]'' | ||
| + | * ''[[tepA]]'' | ||
| + | * ''[[ylzJ]]'' | ||
| + | * ''[[spoIIGA]]'' | ||
| + | * ''[[spoIVFB]]'' | ||
| + | |||
| + | === Additional proteins involved in proteolysis === | ||
* ''[[clpC]]'' | * ''[[clpC]]'' | ||
* ''[[clpE]]'' | * ''[[clpE]]'' | ||
| Line 24: | Line 51: | ||
* ''[[ctpB]]'' | * ''[[ctpB]]'' | ||
* ''[[ctsR]]'' | * ''[[ctsR]]'' | ||
| − | * ''[[ | + | * ''[[ftsH]]'' |
| − | * ''[[ | + | * ''[[htpX]]'' |
| − | |||
* ''[[immA]]'' | * ''[[immA]]'' | ||
* ''[[ipi]]'' | * ''[[ipi]]'' | ||
| + | * ''[[ispA]]'' | ||
* ''[[lonA]]'' | * ''[[lonA]]'' | ||
* ''[[lonB]]'' | * ''[[lonB]]'' | ||
* ''[[mecA]]'' | * ''[[mecA]]'' | ||
* ''[[mlpA]]'' | * ''[[mlpA]]'' | ||
| + | * ''[[prp]]'' | ||
* ''[[prsW]]'' | * ''[[prsW]]'' | ||
* ''[[rasP]]'' | * ''[[rasP]]'' | ||
| − | + | ||
* ''[[yabG]]'' | * ''[[yabG]]'' | ||
* ''[[yirB]]'' | * ''[[yirB]]'' | ||
| Line 44: | Line 72: | ||
* ''[[yraA]]'' | * ''[[yraA]]'' | ||
| − | == | + | == Important reviews == |
| − | + | <pubmed>19421188 23375660 23479438 22688815 24099006 24115457</pubmed> | |
| + | |||
=Back to [[categories]]= | =Back to [[categories]]= | ||
Latest revision as of 12:31, 10 December 2014
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Contents
Genes in this functional category
Protein quality control
Extracellular feeding proteases
- A mutant strain with deletions of all feeding proteases and the three major protein quality control proteases (htrA, htrB, wprA) (BRB14) is available in Colin Harwood's lab PubMed
Proteolysis during sporulation/ germination
Additional proteins involved in proteolysis
- clpC
- clpE
- clpP
- clpQ
- clpX
- clpY
- ctpA
- ctpB
- ctsR
- ftsH
- htpX
- immA
- ipi
- ispA
- lonA
- lonB
- mecA
- mlpA
- prp
- prsW
- rasP
Important reviews
Susanne Pohl, Gaurav Bhavsar, Joanne Hulme, Alexandra E Bloor, Goksel Misirli, Matthew W Leckenby, David S Radford, Wendy Smith, Anil Wipat, E Diane Williamson, Colin R Harwood, Rocky M Cranenburgh
Proteomic analysis of Bacillus subtilis strains engineered for improved production of heterologous proteins.
Proteomics: 2013, 13(22);3298-308
[PubMed:24115457]
[WorldCat.org]
[DOI]
(I p)
Lee Kroos, Yoshinori Akiyama
Biochemical and structural insights into intramembrane metalloprotease mechanisms.
Biochim Biophys Acta: 2013, 1828(12);2873-85
[PubMed:24099006]
[WorldCat.org]
[DOI]
(P p)
Noël Molière, Kürşad Turgay
General and regulatory proteolysis in Bacillus subtilis.
Subcell Biochem: 2013, 66;73-103
[PubMed:23479438]
[WorldCat.org]
[DOI]
(P p)
Aurelia Battesti, Susan Gottesman
Roles of adaptor proteins in regulation of bacterial proteolysis.
Curr Opin Microbiol: 2013, 16(2);140-7
[PubMed:23375660]
[WorldCat.org]
[DOI]
(I p)
Ross E Dalbey, Peng Wang, Jan Maarten van Dijl
Membrane proteases in the bacterial protein secretion and quality control pathway.
Microbiol Mol Biol Rev: 2012, 76(2);311-30
[PubMed:22688815]
[WorldCat.org]
[DOI]
(I p)
Sinisa Urban
Making the cut: central roles of intramembrane proteolysis in pathogenic microorganisms.
Nat Rev Microbiol: 2009, 7(6);411-23
[PubMed:19421188]
[WorldCat.org]
[DOI]
(I p)
