|
rdf:type |
|
|
lifeskim:mentions |
umls-concept:C0009264,
umls-concept:C0033684,
umls-concept:C0035668,
umls-concept:C0035820,
umls-concept:C0036974,
umls-concept:C0043342,
umls-concept:C0205224,
umls-concept:C0524637,
umls-concept:C1514562,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221
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|
pubmed:issue |
47
|
|
pubmed:dateCreated |
1996-1-17
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|
pubmed:abstractText |
The Xenopus Y-box protein FRGY2 has a role in the translational silencing of masked maternal mRNA. Here, we determine that FRGY2 will recognize specific RNA sequences. The evolutionarily conserved nucleic acid-binding cold shock domain is required for sequence-specific interactions with RNA. However, RNA binding by FRGY2 is facilitated by N- and C-terminal regions flanking the cold shock domain. The hydrophilic C-terminal tail domain of FRGY2 interacts with RNA independent of the cold shock domain but does not determine sequence specificity. Thus, both sequence-specific and nonspecific RNA recognition domains are contained within the FRGY2 protein.
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pubmed:language |
eng
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|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Nov
|
|
pubmed:issn |
0021-9258
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
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|
pubmed:day |
24
|
|
pubmed:volume |
270
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
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pubmed:pagination |
28297-303
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|
pubmed:dateRevised |
2010-11-18
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|
pubmed:meshHeading |
pubmed-meshheading:7499328-Amino Acid Sequence,
pubmed-meshheading:7499328-Animals,
pubmed-meshheading:7499328-Base Sequence,
pubmed-meshheading:7499328-Binding Sites,
pubmed-meshheading:7499328-Biological Evolution,
pubmed-meshheading:7499328-Conserved Sequence,
pubmed-meshheading:7499328-DNA Primers,
pubmed-meshheading:7499328-Glutathione Transferase,
pubmed-meshheading:7499328-Molecular Sequence Data,
pubmed-meshheading:7499328-Mutagenesis, Site-Directed,
pubmed-meshheading:7499328-Point Mutation,
pubmed-meshheading:7499328-Polymerase Chain Reaction,
pubmed-meshheading:7499328-RNA,
pubmed-meshheading:7499328-RNA-Binding Proteins,
pubmed-meshheading:7499328-Recombinant Fusion Proteins,
pubmed-meshheading:7499328-Sequence Homology, Amino Acid,
pubmed-meshheading:7499328-Substrate Specificity,
pubmed-meshheading:7499328-Transcription Factors,
pubmed-meshheading:7499328-Xenopus Proteins,
pubmed-meshheading:7499328-Xenopus laevis
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|
pubmed:year |
1995
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|
pubmed:articleTitle |
Sequence-specific RNA recognition by the Xenopus Y-box proteins. An essential role for the cold shock domain.
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|
pubmed:affiliation |
Laboratory of Molecular Embryology, NICHID, National Institutes of Health, Bethesda, Maryland 20892-2710, USA.
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|
pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
|
