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rdf:type |
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lifeskim:mentions |
umls-concept:C0035552,
umls-concept:C0085475,
umls-concept:C0205147,
umls-concept:C0332256,
umls-concept:C1145667,
umls-concept:C1419397,
umls-concept:C1514562,
umls-concept:C1709915,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221
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pubmed:issue |
1
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pubmed:dateCreated |
1999-6-30
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pubmed:abstractText |
In this work we show for the first time that the overproduced N-terminal fragment (residues 1-91) of ribosomal protein TL5 binds specifically to 5S rRNA and that the region of this fragment containing residues 80-91 is a necessity for its RNA-binding activity. The fragment of Escherichia coli 5S rRNA protected by TL5 against RNase A hydrolysis was isolated and sequenced. This 39 nucleotides fragment contains loop E and helices IV and V of 5S rRNA. The isolated RNA fragment forms stable complexes with TL5 and its N-terminal domain. Crystals of TL5 in complex with the RNA fragment diffracting to 2.75 A resolution were obtained.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0014-5793
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
14
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pubmed:volume |
451
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
51-5
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:10356982-Amino Acid Sequence,
pubmed-meshheading:10356982-Bacterial Proteins,
pubmed-meshheading:10356982-Binding Sites,
pubmed-meshheading:10356982-Molecular Sequence Data,
pubmed-meshheading:10356982-Nucleic Acid Conformation,
pubmed-meshheading:10356982-RNA, Ribosomal, 5S,
pubmed-meshheading:10356982-RNA-Binding Proteins,
pubmed-meshheading:10356982-Ribosomal Proteins,
pubmed-meshheading:10356982-Sequence Homology, Amino Acid,
pubmed-meshheading:10356982-Thermus thermophilus
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pubmed:year |
1999
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pubmed:articleTitle |
N-terminal domain, residues 1-91, of ribosomal protein TL5 from Thermus thermophilus binds specifically and strongly to the region of 5S rRNA containing loop E.
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pubmed:affiliation |
Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow Region. gongadze@vega.protres.ru
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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