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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
5
|
| pubmed:dateCreated |
1997-2-14
|
| pubmed:databankReference | |
| pubmed:abstractText |
hnifU, a gene exhibiting similarity to nifU genes of nitrogen fixation gene clusters, was identified in the course of expressed sequence tag (EST) generation from a human fetal heart cDNA library. Northern blot of human tissues and polymerase chain reaction (PCR) using human genomic DNA verified that the hnifU gene represented a human gene rather than a microbial contaminant of the cDNA library. Conceptual translation of the hnifU cDNA yielded a protein product bearing 77% and 70% amino acid identity to NifU-like hypothetical proteins from Haemophilus influenzae and Saccharomyces cerevisiae, respectively, and 40-44% identity to the N-terminal regions of NifU proteins from several diazatrophs (i.e., nitrogen-fixing organisms). Pairwise determination of amino acid identities between the NifU-like proteins of nondiazatrophs showed that these NifU-like proteins exhibited higher sequence identity to each other (63-77%) than to the diazatrophic NifU proteins (40-48%). Further, the NifU-like proteins of non-nitrogen-fixing organisms were similar only to the N-terminal region of diazatrophic NifU proteins and therefore identified a novel modular domain in these NifU proteins. These findings support the hypothesis that NifU is indeed a modular protein. The high degree of sequence similarity between NifU-like proteins from species as divergent as humans and H. influenzae suggests that these proteins perform some basic cellular function and may be among the most highly conserved proteins.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Iron-Sulfur Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/NifU protein, Bacteria,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Nov
|
| pubmed:issn |
0022-2844
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
43
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
536-40
|
| pubmed:dateRevised |
2010-11-18
|
| pubmed:meshHeading |
pubmed-meshheading:8875867-Amino Acid Sequence,
pubmed-meshheading:8875867-Bacterial Proteins,
pubmed-meshheading:8875867-Base Sequence,
pubmed-meshheading:8875867-Cloning, Molecular,
pubmed-meshheading:8875867-Conserved Sequence,
pubmed-meshheading:8875867-DNA, Complementary,
pubmed-meshheading:8875867-Fetal Heart,
pubmed-meshheading:8875867-Gene Expression,
pubmed-meshheading:8875867-Genes,
pubmed-meshheading:8875867-Humans,
pubmed-meshheading:8875867-Iron-Sulfur Proteins,
pubmed-meshheading:8875867-Molecular Sequence Data,
pubmed-meshheading:8875867-Myocardium,
pubmed-meshheading:8875867-Nitrogen Fixation,
pubmed-meshheading:8875867-Organ Specificity,
pubmed-meshheading:8875867-Proteins,
pubmed-meshheading:8875867-RNA, Messenger,
pubmed-meshheading:8875867-Sequence Alignment,
pubmed-meshheading:8875867-Sequence Analysis, DNA,
pubmed-meshheading:8875867-Sequence Homology, Amino Acid,
pubmed-meshheading:8875867-Sequence Homology, Nucleic Acid
|
| pubmed:year |
1996
|
| pubmed:articleTitle |
A modular domain of NifU, a nitrogen fixation cluster protein, is highly conserved in evolution.
|
| pubmed:affiliation |
Department of Clinical Biochemistry, The Centre for Cardiovascular Research, The Toronto Hospital, University of Toronto, Canada.
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|