Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2-3
pubmed:dateCreated
1997-2-19
pubmed:abstractText
The CbpA protein is an analog of the DnaJ molecular chaperone of Escherichia coli. The dnaJ- cbpA- double-null mutant exhibits severe defects in cell growth, namely, a very narrow temperature range for growth. To gain insight into the functions of CbpA as well as DnaJ, we isolated a multicopy suppressor gene that permits this dnaJ- cbpA- mutant to grow normally at low temperatures. The suppressor gene was identified as rpoD, the gene that encodes the major sigma 70. The biological implications of this finding are examined and discussed.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins, http://linkedlifedata.com/resource/pubmed/chemical/CbpA protein, E coli, http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/DNA-Directed RNA Polymerases, http://linkedlifedata.com/resource/pubmed/chemical/DnaJ protein, E coli, http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins, http://linkedlifedata.com/resource/pubmed/chemical/HSP40 Heat-Shock Proteins, http://linkedlifedata.com/resource/pubmed/chemical/HSP70 Heat-Shock Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Heat-Shock Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Molecular Chaperones, http://linkedlifedata.com/resource/pubmed/chemical/RNA polymerase sigma 70, http://linkedlifedata.com/resource/pubmed/chemical/Sigma Factor, http://linkedlifedata.com/resource/pubmed/chemical/dnaK protein, E coli
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0378-1097
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
138
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
245-50
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
The rpoD gene functions as a multicopy suppressor for mutations in the chaperones, CbpA, DnaJ and DnaK, in Escherichia coli.
pubmed:affiliation
Laboratory of Molecular Microbiology, School of Agriculture, Nagoya University, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't