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Membrane-bound thiol-disulfide oxidoreductases in Bacillus subtilis

Erlendsson, Lydur LU (2003)
Abstract
Disulfide bonds in proteins are found between cysteine residues and are usually important for either function or stability of proteins. Thiol-disulfide oxidoreductases catalyse the formation or breakage of disulfide bonds in proteins. The gram-positive endospore-forming bacterium Bacillus subtilis contains several membrane-bound thiol-disulfide oxidoreductases. BdbA, BdbB and CcdA have been described before. In this thesis BdbC, BdbD, ResA and StoA have been identified and studied.



·BdbD catalyses disulfide bond formation in proteins on the outer side of the cytoplasmic membrane and BdbC re-oxidises BdbD.



·BdbA and BdbB are apparent homologues of BdbD and BdbC, respectively. They appear to by specific... (More)
Disulfide bonds in proteins are found between cysteine residues and are usually important for either function or stability of proteins. Thiol-disulfide oxidoreductases catalyse the formation or breakage of disulfide bonds in proteins. The gram-positive endospore-forming bacterium Bacillus subtilis contains several membrane-bound thiol-disulfide oxidoreductases. BdbA, BdbB and CcdA have been described before. In this thesis BdbC, BdbD, ResA and StoA have been identified and studied.



·BdbD catalyses disulfide bond formation in proteins on the outer side of the cytoplasmic membrane and BdbC re-oxidises BdbD.



·BdbA and BdbB are apparent homologues of BdbD and BdbC, respectively. They appear to by specific for disulfide bond formation in the lanthionine Sublancin 168.



·ResA functions in cytochrome c synthesis.



·CcdA is involved in cytochrome c synthesis and endospore formation.



·StoA plays a role in endospore biogenesis. (Less)
Please use this url to cite or link to this publication:
author
opponent
  • Dr. Thöny-Meyer, Linda, ETH, Zurich, Switzerland
organization
publishing date
type
Thesis
publication status
published
subject
keywords
virologi, mykologi, Mikrobiologi, mycology, virology, bacteriology, Microbiology, sporulation, cytochrome c, thiol-disulfide oxidoreductases, Bacillus subtilis, membrane proteins, bakteriologi
pages
120 pages
publisher
Lydur Erlendsson, Department of cell and organsimbiology, Sölvegatan 35, Lund,
defense location
Biologihörsalen, Sölvegatan 35, Lund
defense date
2004-01-17 10:15
ISBN
91-85067-09-1
language
English
LU publication?
yes
id
2928ecc6-5abd-40f5-a3fa-17a060045510 (old id 466555)
date added to LUP
2007-09-28 12:12:41
date last changed
2016-09-19 08:45:08
@phdthesis{2928ecc6-5abd-40f5-a3fa-17a060045510,
  abstract     = {Disulfide bonds in proteins are found between cysteine residues and are usually important for either function or stability of proteins. Thiol-disulfide oxidoreductases catalyse the formation or breakage of disulfide bonds in proteins. The gram-positive endospore-forming bacterium Bacillus subtilis contains several membrane-bound thiol-disulfide oxidoreductases. BdbA, BdbB and CcdA have been described before. In this thesis BdbC, BdbD, ResA and StoA have been identified and studied.<br/><br>
<br/><br>
·BdbD catalyses disulfide bond formation in proteins on the outer side of the cytoplasmic membrane and BdbC re-oxidises BdbD.<br/><br>
<br/><br>
·BdbA and BdbB are apparent homologues of BdbD and BdbC, respectively. They appear to by specific for disulfide bond formation in the lanthionine Sublancin 168.<br/><br>
<br/><br>
·ResA functions in cytochrome c synthesis.<br/><br>
<br/><br>
·CcdA is involved in cytochrome c synthesis and endospore formation.<br/><br>
<br/><br>
·StoA plays a role in endospore biogenesis.},
  author       = {Erlendsson, Lydur},
  isbn         = {91-85067-09-1},
  keyword      = {virologi,mykologi,Mikrobiologi,mycology,virology,bacteriology,Microbiology,sporulation,cytochrome c,thiol-disulfide oxidoreductases,Bacillus subtilis,membrane proteins,bakteriologi},
  language     = {eng},
  pages        = {120},
  publisher    = {Lydur Erlendsson, Department of cell and organsimbiology, Sölvegatan 35, Lund,},
  school       = {Lund University},
  title        = {Membrane-bound thiol-disulfide oxidoreductases in Bacillus subtilis},
  year         = {2003},
}