Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2003-5-6
pubmed:abstractText
Fe-S clusters are key to the sensing and transcription functions of three transcription factors, FNR, IscR and SoxR. All three proteins were discovered in Escherichia coli but experimental data and bioinformatic predictions suggest that homologs of these proteins exist in other bacterial species, highlighting the widespread nature of Fe-S-dependent regulatory networks. In addition, the nearly ubiquitous citric acid cycle enzyme, aconitase, plays a role in translational regulation in E. coli and Bacillus subtilis when it loses its Fe-S cluster. Although these regulatory proteins have the common feature of containing an Fe-S cluster, they differ in the physiological signals that they respond to. Therefore, these regulatory factors provide insights into the chemical versatility of Fe-S clusters.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
1369-5274
pubmed:author
pubmed:issnType
Print
pubmed:volume
6
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
181-5
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
2003
pubmed:articleTitle
The role of Fe-S proteins in sensing and regulation in bacteria.
pubmed:affiliation
Department of Biomolecular Chemistry, Medical School, University of Wisconsin, 1300 University Avenue, Madison, Wisconsin 53706, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Review