YTH: a new domain in nuclear proteins

A novel 100–150-residue domain has been identified in the human splicing factor YT521-B and its Drosophila and yeast homologues. Homology searches show that the domain is typical for the eukaryotes and is particularly abundant in plants. It is predicted to adopt a mixed α-helix–β-sheet fold and to b...

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Bibliographic Details
Published in:	Trends in biochemical sciences (Amsterdam. Regular ed.) Vol. 27; no. 10; pp. 495 - 497
Main Authors:	Stoilov, Peter, Rafalska, Ilona, Stamm, Stefan
Format:	Journal Article
Language:	English
Published:	England Elsevier Ltd 01-10-2002
Subjects:	alternative splicing Amino Acid Sequence Animals Humans Molecular Sequence Data nuclear proteins Nuclear Proteins - analysis Nuclear Proteins - chemistry pre-mRNA processing Protein Structure, Secondary Protein Structure, Tertiary RNA Splicing - physiology Saccharomyces cerevisiae - metabolism Sequence Alignment Sequence Homology, Amino Acid YT521-B YTH domain alternative splicing Techniques & Methods Structural Biology pre-mRNA processing Genetics YT521-B Biochemistry YTH domain nuclear proteins
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Summary:	A novel 100–150-residue domain has been identified in the human splicing factor YT521-B and its Drosophila and yeast homologues. Homology searches show that the domain is typical for the eukaryotes and is particularly abundant in plants. It is predicted to adopt a mixed α-helix–β-sheet fold and to bind to RNA. We propose the name YTH (for YT521-B homology) for the domain. We report the identification of a new domain in splicing factor YT521-B and a number of proteins of unknown function that could be involved in RNA binding.
Bibliography:	ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 ObjectType-Review-3 content type line 23 ObjectType-Feature-3 ObjectType-Review-1
ISSN:	0968-0004 1362-4326
DOI:	10.1016/S0968-0004(02)02189-8