Linked Life Data

8253388

Source:http://linkedlifedata.com/resource/pubmed/id/8253388

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
12A
pubmed:dateCreated
1994-1-13
pubmed:databankReference
pubmed:abstractText
Nuclear respiratory factor 1 (NRF-1) was first discovered as an activator of the cytochrome c gene and was subsequently found to play a broader role in nuclear-mitochondrial interactions. We have now cloned a HeLa cDNA encoding NRF-1 using degenerate oligomers derived from tryptic peptide sequences for PCR amplification. The cDNA-encoded protein was indistinguishable from the authentic HeLa cell factor on denaturing gels, displayed the expected NRF-1 DNA-binding specificity, and made the same guanine nucleotide contacts as HeLa NRF-1 on binding known NRF-1 recognition sites. Antiserum raised against the highly purified recombinant protein recognized the identical DNA-protein complex formed using either a crude nuclear fraction or nearly homogeneous HeLa NRF-1. Recombinant NRF-1 also activated transcription through specific sites from several NRF-1-responsive promoters, confirming both the transcriptional activity and specificity of the cDNA product. Portions of NRF-1 are closely related to sea urchin P3A2 and the erect wing (EWG) protein of Drosophila. Both are recently identified developmental regulatory factors. The region of highest sequence identity with P3A2 and EWG was in the amino-terminal half of the molecule, which was found by deletion mapping to contain the DNA-binding domain, whereas the carboxy-terminal half of NRF-1 was highly divergent from both proteins. The DNA-binding domain in these molecules is unrelated to motifs found commonly in DNA-binding proteins; thus, NRF-1, P3A2, and EWG represent the founding members of a new class of highly conserved sequence-specific regulatory factors.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0890-9369
pubmed:author
pubmed:issnType
Print
pubmed:volume
7
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2431-45
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
NRF-1, an activator involved in nuclear-mitochondrial interactions, utilizes a new DNA-binding domain conserved in a family of developmental regulators.
pubmed:affiliation
Department of Cell, Molecular, and Structural Biology, Northwestern University Medical School, Chicago, Illinois 60611.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't