Cysteine desulphurase plays an important role in environmental adaptation of the hyperthermophilic archaeon Thermococcus kodakarensis. Issue 2 (24th June 2014)
- Record Type:
- Journal Article
- Title:
- Cysteine desulphurase plays an important role in environmental adaptation of the hyperthermophilic archaeon Thermococcus kodakarensis. Issue 2 (24th June 2014)
- Main Title:
- Cysteine desulphurase plays an important role in environmental adaptation of the hyperthermophilic archaeon Thermococcus kodakarensis
- Authors:
- Hidese, Ryota
Inoue, Takahiro
Imanaka, Tadayuki
Fujiwara, Shinsuke - Abstract:
- <abstract abstract-type="main"> <title>Summary</title> <p>The sulphur atoms of sulphur‐containing cofactors that are essential for numerous cellular functions in living organisms originate from L‐cysteine via cysteine desulphurase (CSD) activity. However, many (hyper)thermophilic archaea, which thrive in solfataric fields and are positioned near the root of the evolutionary tree of life, lack CSD orthologues. The existence of CSD orthologues in a subset of (hyper)thermophilic archaea is of interest with respect to the evolution of sulphur‐trafficking systems for the cofactors. This study demonstrates that the disruption of the <italic>csd</italic> gene of <italic>T</italic><italic>hermococcus kodakarensis</italic>, a facultative elemental sulphur (S<sup>0</sup>)‐reducing hyperthermophilic archaeon, encoding <italic>Tk</italic>‐CSD, conferred a growth defect evident only in the absence of S<sup>0</sup>, and that growth can be restored by the addition of S<sup>0</sup>, but not sulphide. We show that the <italic>csd</italic> gene is not required for biosynthesis of thiamine pyrophosphate or molybdopterin, irrespective of the presence or absence of S<sup>0</sup>, but is necessary for iron‐sulphur cluster biosynthesis in the absence of S<sup>0</sup>. Recombinant form of <italic>Tk</italic>‐CSD expressed in <italic>E</italic><italic>scherichia coli</italic> was obtained and it was found to catalyse the desulphuration of L‐cysteine. The obtained data suggest that hyperthermophiles<abstract abstract-type="main"> <title>Summary</title> <p>The sulphur atoms of sulphur‐containing cofactors that are essential for numerous cellular functions in living organisms originate from L‐cysteine via cysteine desulphurase (CSD) activity. However, many (hyper)thermophilic archaea, which thrive in solfataric fields and are positioned near the root of the evolutionary tree of life, lack CSD orthologues. The existence of CSD orthologues in a subset of (hyper)thermophilic archaea is of interest with respect to the evolution of sulphur‐trafficking systems for the cofactors. This study demonstrates that the disruption of the <italic>csd</italic> gene of <italic>T</italic><italic>hermococcus kodakarensis</italic>, a facultative elemental sulphur (S<sup>0</sup>)‐reducing hyperthermophilic archaeon, encoding <italic>Tk</italic>‐CSD, conferred a growth defect evident only in the absence of S<sup>0</sup>, and that growth can be restored by the addition of S<sup>0</sup>, but not sulphide. We show that the <italic>csd</italic> gene is not required for biosynthesis of thiamine pyrophosphate or molybdopterin, irrespective of the presence or absence of S<sup>0</sup>, but is necessary for iron‐sulphur cluster biosynthesis in the absence of S<sup>0</sup>. Recombinant form of <italic>Tk</italic>‐CSD expressed in <italic>E</italic><italic>scherichia coli</italic> was obtained and it was found to catalyse the desulphuration of L‐cysteine. The obtained data suggest that hyperthermophiles might benefit from a capacity for CSD‐dependent iron‐sulphur cluster biogenesis, which allows them to thrive outside solfataric environments.</p> </abstract> … (more)
- Is Part Of:
- Molecular microbiology. Volume 93:Issue 2(2014)
- Journal:
- Molecular microbiology
- Issue:
- Volume 93:Issue 2(2014)
- Issue Display:
- Volume 93, Issue 2 (2014)
- Year:
- 2014
- Volume:
- 93
- Issue:
- 2
- Issue Sort Value:
- 2014-0093-0002-0000
- Page Start:
- 331
- Page End:
- 345
- Publication Date:
- 2014-06-24
- Subjects:
- Molecular microbiology -- Periodicals
572.829 - Journal URLs:
- http://www.blackwell-synergy.com/servlet/useragent?func=showIssues&code=mmi&close=2003#C2003 ↗
http://onlinelibrary.wiley.com/journal/10.1111/(ISSN)1365-2958 ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1111/mmi.12662 ↗
- Languages:
- English
- ISSNs:
- 0950-382X
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 5900.817960
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 3093.xml