Linked Life Data

10997488

Source:http://linkedlifedata.com/resource/pubmed/id/10997488

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2000-12-21
pubmed:abstractText
The Escherichia coli PrmA enzyme catalyzes methylation of the large ribosomal subunit protein L11. Database homology searches, multiple sequence alignment, and structure prediction allowed to dissect the primary structure of PrmA into two domains and assign putative functional or structural roles to invariant or highly conserved residues. Evolutionary relationships within the PrmA family were also analyzed. The topology of the branching order agrees to a large extent with the consensus phylogeny of Eubacteria, with the exception of beta and epsilon subdivisions of Proteobacteria, which most probably had their original prmA genes replaced by copies acquired via the lateral gene transfer from gamma-Proteobacteria and some close relative of the ancestor of gramnegative bacteria, respectively.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0137-1320
pubmed:author
pubmed:issnType
Print
pubmed:volume
49
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
19-29
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2000
pubmed:articleTitle
Sequence, structural, and evolutionary analysis of prokaryotic ribosomal protein L11 methyltransferases.
pubmed:affiliation
Henry Ford Health System, Molecular Biology Research Program, Detroit, MI 48202, USA. iamb@bioinfo.pl
pubmed:publicationType
Journal Article