Linked Life Data

10572294

Source:http://linkedlifedata.com/resource/pubmed/id/10572294

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8-9
pubmed:dateCreated
2000-1-6
pubmed:abstractText
Functional domains of the initiator protein DnaA of Escherichia coli have been defined. Domain 1, amino acids 1-86, is involved in oligomerization and in interaction with DnaB. Domain 2, aa 87-134, constitutes a flexible loop. Domain 3, aa 135-373, contains the binding site for ATP or ADP, the ATPase function, a second interaction site with DnaB, and is required for local DNA unwinding. Domain 4 is required and sufficient for specific binding to DNA. We show that there are three different types of cooperative interactions during the DNA binding of DnaA proteins from E. coli, Streptomyces lividans, and Thermus thermophilus: i) binding to distant binding sites; ii) binding to closely spaced binding sites; and iii) binding to non-canonical binding sites.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0300-9084
pubmed:author
pubmed:issnType
Print
pubmed:volume
81
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
819-25
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:articleTitle
Functional domains of DnaA proteins.
pubmed:affiliation
Max-Planck-Institut für molekulare Genetik, Ihnestrasse 73, 14195 Berlin-Dahlem, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't