rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
3
|
pubmed:dateCreated |
1991-5-21
|
pubmed:databankReference |
|
pubmed:abstractText |
Using lambda phage clones containing segments of the Escherichia coli K12 chromosome as hybridization probes, we found one gene at 42 min on the E. coli chromosome map, the expression of which was affected by RNase III. The sequence of the DNA fragment containing this gene (gen-165) revealed the presence of an open reading frame encoding a polypeptide of 165 amino acid residues. The amino acid sequence deduced from the nucleotide sequence exhibited a remarkable similarity to that of the human ferritin H chain.
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Mar
|
pubmed:issn |
0026-8925
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:volume |
225
|
pubmed:geneSymbol |
gen-165
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
510-3
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading |
pubmed-meshheading:2017145-Amino Acid Sequence,
pubmed-meshheading:2017145-Base Sequence,
pubmed-meshheading:2017145-Blotting, Northern,
pubmed-meshheading:2017145-Chromosome Mapping,
pubmed-meshheading:2017145-Chromosomes, Bacterial,
pubmed-meshheading:2017145-Cloning, Molecular,
pubmed-meshheading:2017145-DNA,
pubmed-meshheading:2017145-DNA, Bacterial,
pubmed-meshheading:2017145-Endoribonucleases,
pubmed-meshheading:2017145-Escherichia coli,
pubmed-meshheading:2017145-Escherichia coli Proteins,
pubmed-meshheading:2017145-Ferritins,
pubmed-meshheading:2017145-Genes, Bacterial,
pubmed-meshheading:2017145-Humans,
pubmed-meshheading:2017145-Molecular Sequence Data,
pubmed-meshheading:2017145-Open Reading Frames,
pubmed-meshheading:2017145-Restriction Mapping,
pubmed-meshheading:2017145-Ribonuclease III,
pubmed-meshheading:2017145-Sequence Homology, Nucleic Acid
|
pubmed:year |
1991
|
pubmed:articleTitle |
Cloning and sequencing of an Escherichia coli K12 gene which encodes a polypeptide having similarity to the human ferritin H subunit.
|
pubmed:affiliation |
Department of Biology, Saga Medical School, Nabeshima, Japan.
|
pubmed:publicationType |
Journal Article,
Comparative Study
|