Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
38
|
pubmed:dateCreated |
1995-11-6
|
pubmed:abstractText |
The role of the 2'-hydroxyl group in RNA--protein interaction has been investigated using MS2 coat protein and its hairpin RNA operator as a model system. Derivatives of the MS2 translational operator were prepared where individual riboses were replaced by deoxyribose and their binding affinities to MS2 coat protein were determined. Only 1 (U-5) out of 15 positions tested reduced protein affinity by 1.6 kcal/mol. A variety of other 2'-modifications were tested at this position to understand the role of this particular 2'-hydroxyl group. Normal binding of the U-NH2 variant and weaker binding of the U-O-methyl variant are consistent with the ability of these functional groups to provide a hydrogen bond donor. This is also supported by recent crystallographic data which indicate a possible interaction between the 2'-hydroxyl of U-5 and the carboxylate group of glutamate 63 [Valegård et al. (1994) Nature 371, 623-626]. Complementary experiments introducing riboses into a DNA hairpin confirm the putative protein contact, and also identify a requirement for riboses in the two upper base pairs of the hairpin. Several arguments suggest these riboses are required to maintain an A-form helix in this region of the binding site. A minimum requirement of four 2'-hydroxyl groups for wild-type coat protein binding has been determined, one of which is at the -5 position and other three in the upper stem in any combination.(ABSTRACT TRUNCATED AT 250 WORDS)
|
pubmed:grant | |
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Capsid Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/Deoxyribonucleotides,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Viral,
http://linkedlifedata.com/resource/pubmed/chemical/RNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Ribose
|
pubmed:status |
MEDLINE
|
pubmed:month |
Sep
|
pubmed:issn |
0006-2960
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
26
|
pubmed:volume |
34
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
12363-8
|
pubmed:dateRevised |
2007-11-14
|
pubmed:meshHeading |
pubmed-meshheading:7547980-Base Sequence,
pubmed-meshheading:7547980-Capsid,
pubmed-meshheading:7547980-Capsid Proteins,
pubmed-meshheading:7547980-DNA,
pubmed-meshheading:7547980-Deoxyribonucleotides,
pubmed-meshheading:7547980-Models, Molecular,
pubmed-meshheading:7547980-Molecular Sequence Data,
pubmed-meshheading:7547980-Nucleic Acid Conformation,
pubmed-meshheading:7547980-Protein Binding,
pubmed-meshheading:7547980-RNA, Viral,
pubmed-meshheading:7547980-RNA-Binding Proteins,
pubmed-meshheading:7547980-Ribose,
pubmed-meshheading:7547980-Structure-Activity Relationship
|
pubmed:year |
1995
|
pubmed:articleTitle |
The role of 2'-hydroxyl groups in an RNA-protein interaction.
|
pubmed:affiliation |
Department of Chemistry and Biochemistry, University of Colorado, Boulder 80309-0215, USA.
|
pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|