Linked Life Data

9742254

Source:http://linkedlifedata.com/resource/pubmed/id/9742254

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
19
pubmed:dateCreated
1998-11-17
pubmed:abstractText
The VP16 protein of herpes simplex virus is a potent transcriptional activator of the viral immediate early genes. The transcriptional activation region of VP16 can be divided into two functional subregions, here designated VP16N (comprising amino acids 413-456) and VP16C (amino acids 450-490). Assays of VP16C mutants resulting from both random and alanine-scanning mutagenesis indicated that the sidechains of three phenylalanines (at positions 473, 475 and 479) and one acidic residue (glutamate 476) are important for transcriptional activation. Aromatic and bulky hydrophobic amino acids were effective substitutes for each of the three Phe residues, whereas replacement with smaller or polar amino acids resulted in loss of transcriptional function. In contrast, many changes were tolerated for Glu476, including bulky hydrophobic and basic amino acids, indicating that the negative charge at this position contributes little to the function of this subregion. Similar relative activities for most of the mutants were observed in yeast and in mammalian cells, indicating that the structural requirements for this activation region are comparable in these two species. These results reinforce the hypothesis that bulky hydrophobic residues, not acidic residues, are most critical for the activity of this 'acidic' transcriptional activation region.
pubmed:grant
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0305-1048
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
26
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4487-96
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
Mutational analysis of a transcriptional activation region of the VP16 protein of herpes simplex virus.
pubmed:affiliation
Department of Biochemistry, Michigan State University, East Lansing, MI 48824-1319, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't