Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2003-6-27
pubmed:abstractText
Large subunits of NiFe-hydrogenases undergo a unique maturation process in which the last step consists of the endoproteolytic cleavage of the C-terminal extension after the Ni-Fe metal center has been assembled. To assess in vivo the influence of alteration of the C-terminal extension on the processing, green fluorescence protein (GFP) was fused to the C-terminus of the large subunit (HybC) of the Escherichia coli hydrogenase 2. Interestingly, no processing of HybC-GFP was observed. In addition, the chromophore of GFP was not formed, implying a nonproductive folding of the upstream HybC moiety. These results strongly suggest that the alteration of the C-terminus of the hydrogenase 2 large subunit interferes with the folding and processing of HybC.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0300-9084
pubmed:author
pubmed:issnType
Print
pubmed:volume
85
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
575-9
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
2003
pubmed:articleTitle
Effect of alteration of the C-terminal extension on the maturation and folding of the large subunit of the Escherichia coli hydrogenase-2.
pubmed:affiliation
Laboratoire de Chimie Bactérienne, UPR9043 CNRS, Institut de Biologie Structurale et Microbiologie, 31 chemin Joseph Aiguier, 13402 Marseille cedex 20, France.
pubmed:publicationType
Journal Article, In Vitro, Research Support, Non-U.S. Gov't