Difference between revisions of "Proteolysis"
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* ''[[htrA]]'' | * ''[[htrA]]'' | ||
* ''[[htrB]]'' | * ''[[htrB]]'' | ||
| + | * ''[[htrC]]'' | ||
* ''[[wprA]]'' | * ''[[wprA]]'' | ||
| − | === | + | === Extracellular feeding proteases === |
| + | * [[AprE]] and [[NprE]] account for 95% of extracellular proteolytic activity | ||
| + | |||
| + | * ''[[aprE]]'' | ||
* ''[[bpr]]'' | * ''[[bpr]]'' | ||
* ''[[epr]]'' | * ''[[epr]]'' | ||
* ''[[mpr]]'' | * ''[[mpr]]'' | ||
* ''[[nprB]]'' | * ''[[nprB]]'' | ||
| + | * ''[[nprE]]'' | ||
* ''[[vpr]]'' | * ''[[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]] === | === Proteolysis during [[sporulation]]/ [[germination]] === | ||
| Line 53: | Line 60: | ||
* ''[[mecA]]'' | * ''[[mecA]]'' | ||
* ''[[mlpA]]'' | * ''[[mlpA]]'' | ||
| + | * ''[[prp]]'' | ||
* ''[[prsW]]'' | * ''[[prsW]]'' | ||
* ''[[rasP]]'' | * ''[[rasP]]'' | ||
| Line 63: | Line 71: | ||
* ''[[yqgP]]'' | * ''[[yqgP]]'' | ||
* ''[[yraA]]'' | * ''[[yraA]]'' | ||
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== Important reviews == | == Important reviews == | ||
| − | <pubmed>19421188 23375660 23479438 22688815 </pubmed> | + | <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)
