Linked Life Data

6179777

Source:http://linkedlifedata.com/resource/pubmed/id/6179777

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1982-10-12
pubmed:abstractText
A new endoribonuclease activity, RNase F, was partially purified from Escherichia coli cells. This activity can specifically cleave a precursor RNA molecule (of species 1) isolated from T4-infected cells [N. Watson & D. Apirion (1981) Biochem. Biophys. Res. Commun. 103, 543-551]. The cleavage results in products which are very similar to RNA molecules found in the cell, generating a 3'-phosphate and a 5'-hydroxyl groups. The cleavage takes place between a cytosine and an adenine moiety, within a possible loop and stem structure; the cut is in the border between the double-stranded and single-stranded regions of this structure. This specificity of this enzyme could be the introduction of a cleavage near the 3' ends of tRNA molecules and other RNAs like species 1 which could resemble tRNA in their three-dimensional structure.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:volume
124
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
553-9
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1982
pubmed:articleTitle
A cleavage site of ribonuclease F. A putative processing endoribonuclease from Escherichia coli.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.