Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1991-10-25
pubmed:abstractText
The RNA polymerase core enzyme of Escherichia coli has the subunit composition alpha 2 beta beta', and when combined with one of several alternative sigma-subunits (initiation-specificity) produces holoenzyme capable of all the steps of transcription. Dimerization of the alpha-subunit and association with the beta-subunit trigger assembly of the core enzyme. Analyses of a set of deletion derivatives of rpoA (which encodes alpha) have indicated that as many as 94 carboxy-terminal amino acids (but not 153) can be removed without preventing assembly of core-like complexes in vitro. Detailed analyses of these deletion mutants have now been performed in vivo. alpha-Polypeptides truncated from the carboxy terminus to amino acid residues 235, 256 or 296 are assembled not merely into core, but also into holoenzyme-like complexes in vivo, and at least in the first two cases both of the two alpha-subunits can be replaced by the truncated versions. Nevertheless, none can complement rpoAts alleles for growth at 42 degrees C. We conclude that the domain(s) of alpha essential for the assembly of RNA polymerase (at least the major holoenzyme species) are confined to the amino-terminal 235 amino acids, while some other essential function(s) require residues close to the carboxy terminus.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0022-2836
pubmed:author
pubmed:issnType
Print
pubmed:day
5
pubmed:volume
221
pubmed:geneSymbol
rpoA
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
23-9
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
Functional specialization within the alpha-subunit of Escherichia coli RNA polymerase.
pubmed:affiliation
Department of Molecular Genetics, National Institute of Genetics, Shizuoka, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't