Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1992-2-6
pubmed:databankReference
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/J01654, http://linkedlifedata.com/resource/pubmed/xref/GENBANK/J01714, http://linkedlifedata.com/resource/pubmed/xref/GENBANK/J01787, http://linkedlifedata.com/resource/pubmed/xref/GENBANK/J01792, http://linkedlifedata.com/resource/pubmed/xref/GENBANK/J01811, http://linkedlifedata.com/resource/pubmed/xref/GENBANK/K00030, http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M63353, http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M63355, http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M63368, http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M63369, http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M63371, http://linkedlifedata.com/resource/pubmed/xref/GENBANK/X00618, http://linkedlifedata.com/resource/pubmed/xref/GENBANK/X02006, http://linkedlifedata.com/resource/pubmed/xref/GENBANK/X02603, http://linkedlifedata.com/resource/pubmed/xref/GENBANK/X02604, http://linkedlifedata.com/resource/pubmed/xref/GENBANK/X02605, http://linkedlifedata.com/resource/pubmed/xref/GENBANK/X02662
pubmed:abstractText
Synonymous and nonsynonymous substitution rates at the loci encoding glyceraldehyde-3-phosphate dehydrogenase (gap) and outer membrane protein 3A (ompA) were examined in 12 species of enteric bacteria. By examining homologous sequences in species of varying degrees of relatedness and of known phylogenetic relationships, we analyzed the patterns of synonymous and nonsynonymous substitutions within and among these genes. Although both loci accumulate synonymous substitutions at reduced rates due to codon usage bias, portions of the gap and ompA reading frames show significant deviation in synonymous substitution rates not attributable to local codon bias. A paucity of synonymous substitutions in portions of the ompA gene may reflect selection for a novel mRNA secondary structure. In addition, these studies allow comparisons of homologous protein-coding sequences (gap) in plants, animals, and bacteria, revealing differences in evolutionary constraints on this glycolytic enzyme in these lineages.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0022-2844
pubmed:author
pubmed:issnType
Print
pubmed:volume
33
pubmed:geneSymbol
gap, ompA
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
241-50
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
Molecular considerations in the evolution of bacterial genes.
pubmed:affiliation
Department of Genetics, Washington University School of Medicine, St. Louis, MO 63110.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S.