Linked Life Data

6248523

Source:http://linkedlifedata.com/resource/pubmed/id/6248523

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
13
pubmed:dateCreated
1980-9-28
pubmed:abstractText
A protein that binds tightly to single-stranded but not to double-strained nucleic acids has been purified to homogeneity from a high salt wash of ribosomes from cryptobiotic Artemia saline gastrulae. The protein, designated HD40 to indicate a helix-destabilizing protein with a molecular weight of 40,000, is present in the high-salt ribosomal wash at a level of about 2 molecules per 80 S ribosome. The protein is monomeric at salt concentrations from 0.01 to 0.5 M and has an alpha-helix content of approximately 15%. The amino acid composition of HD40 is characterized by a high glycine content (19.5 mol%), the absence of cysteine, and the presence of the unusual amino acid dimethylarginine. The isolated protein binds preferentially to natural RNA over denatured DNA. HD40 inhibits protein synthesis directed by poly(rU) and by Artemia poly(A+) RNA in cell-free systems derived from Artemia and from wheat germ; inhibition is relieved by excess of mRNA. Single-stranded ribo- and deoxyribopolynucleotides are largely protected from degradation by nucleases when complexed with HD40.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
255
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
6466-72
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1980
pubmed:articleTitle
A single-stranded nucleic acid-binding protein from Artemia salina. I. Purification and characterization.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.