Linked Life Data

10821700

Source:http://linkedlifedata.com/resource/pubmed/id/10821700

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
20
pubmed:dateCreated
2000-6-21
pubmed:abstractText
The carboxy-terminal domain of the alpha subunit of Escherichia coli RNA polymerase, which is connected with the core part of RNA polymerase through a long flexible linker, plays decisive roles in transcription activation by directly interacting with a large number of transcription factors and upstream (UP) element DNA. Here we constructed a set of mutant RNA polymerases, each containing a mutant alpha subunit with an altered interdomain linker. Deletion of three amino acids from the linker exhibited 50% inhibition of cAMP receptor protein- (CRP-) dependent lac P1 transcription. Deletion of six amino acids completely knocked out the activity. Insertion of three amino acids did not affect the activity, whereas 40-60% inhibition was observed after insertion of one, two, or four amino acids. Substitution of 10 consecutive glycine residues resulted in nearly 90% reduction of the CRP-dependent activity, whereas 50% activity was retained after substitution of 10 proline residues or a sequence expected to form a strong alpha-helix. Essentially the same results were obtained with UP element-dependent rrnB P1 transcription. These observations altogether suggest that (i) sufficient length of the interdomain linker is required for transcription activation mediated by the alpha carboxy-terminal domain, (ii) the linker is not totally unstructured but has structural and torsional preferences to facilitate positioning of the carboxy-terminal domain to a proper location for the interaction with CRP and UP element, and (iii) CRP-dependent activation and UP element-dependent activation share a common intermediary state in which the positioning of the alpha carboxy-terminal domain is of primary importance.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
23
pubmed:volume
39
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
6243-9
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:10821700-5' Untranslated Regions, pubmed-meshheading:10821700-Amino Acid Sequence, pubmed-meshheading:10821700-Amino Acid Substitution, pubmed-meshheading:10821700-Base Sequence, pubmed-meshheading:10821700-Cyclic AMP Receptor Protein, pubmed-meshheading:10821700-DNA-Directed RNA Polymerases, pubmed-meshheading:10821700-Escherichia coli, pubmed-meshheading:10821700-Lac Operon, pubmed-meshheading:10821700-Molecular Sequence Data, pubmed-meshheading:10821700-Mutagenesis, Site-Directed, pubmed-meshheading:10821700-Peptide Fragments, pubmed-meshheading:10821700-Promoter Regions, Genetic, pubmed-meshheading:10821700-Protein Structure, Tertiary, pubmed-meshheading:10821700-Structure-Activity Relationship, pubmed-meshheading:10821700-Transcription, Genetic, pubmed-meshheading:10821700-rRNA Operon
pubmed:year
2000
pubmed:articleTitle
Structural requirements for the interdomain linker of alpha subunit of Escherichia coli RNA polymerase.
pubmed:affiliation
Department of Molecular Genetics, National Institute of Genetics, 1111 Yata, Mishima, Shizuoka 411-8540, Japan. nfujita@lab.nig.ac.jp
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't