Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2008-12-29
pubmed:databankReference
pubmed:abstractText
PUF60 is an essential splicing factor functionally related and homologous to U2AF(65). Its C-terminal domain belongs to the family of U2AF (U2 auxiliary factor) homology motifs (UHM), a subgroup of RNA recognition motifs that bind to tryptophan-containing linear peptide motifs (UHM ligand motifs, ULMs) in several nuclear proteins. Here, we show that the Puf60 UHM is mainly monomeric in physiological buffer, whereas its dimerization is induced upon the addition of SDS. The crystal structure of PUF60-UHM at 2.2 angstroms resolution, NMR data, and mutational analysis reveal that the dimer interface is mediated by electrostatic interactions involving a flexible loop. Using glutathione S-transferase pulldown experiments, isothermal titration calorimetry, and NMR titrations, we find that Puf60-UHM binds to ULM sequences in the splicing factors SF1, U2AF65, and SF3b155. Compared with U2AF65-UHM, Puf60-UHM has distinct binding preferences to ULMs in the N terminus of SF3b155. Our data suggest that the functional cooperativity between U2AF65 and Puf60 may involve simultaneous interactions of the two proteins with SF3b155.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins, http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins, http://linkedlifedata.com/resource/pubmed/chemical/Ribonucleoprotein, U2 Small Nuclear, http://linkedlifedata.com/resource/pubmed/chemical/Ribonucleoproteins, http://linkedlifedata.com/resource/pubmed/chemical/SF1 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/SF3B1 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/SIAHBP1 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Sodium Dodecyl Sulfate, http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors, http://linkedlifedata.com/resource/pubmed/chemical/splicing factor U2AF
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
2
pubmed:volume
284
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
630-9
pubmed:meshHeading
pubmed-meshheading:18974054-Amino Acid Motifs, pubmed-meshheading:18974054-Animals, pubmed-meshheading:18974054-Carrier Proteins, pubmed-meshheading:18974054-Crystallography, X-Ray, pubmed-meshheading:18974054-DNA-Binding Proteins, pubmed-meshheading:18974054-Dimerization, pubmed-meshheading:18974054-Humans, pubmed-meshheading:18974054-Nuclear Magnetic Resonance, Biomolecular, pubmed-meshheading:18974054-Nuclear Proteins, pubmed-meshheading:18974054-Phosphoproteins, pubmed-meshheading:18974054-Protein Binding, pubmed-meshheading:18974054-Protein Structure, Quaternary, pubmed-meshheading:18974054-Protein Structure, Tertiary, pubmed-meshheading:18974054-Ribonucleoprotein, U2 Small Nuclear, pubmed-meshheading:18974054-Ribonucleoproteins, pubmed-meshheading:18974054-Sequence Homology, Amino Acid, pubmed-meshheading:18974054-Sodium Dodecyl Sulfate, pubmed-meshheading:18974054-Transcription Factors
pubmed:year
2009
pubmed:articleTitle
Dimerization and protein binding specificity of the U2AF homology motif of the splicing factor Puf60.
pubmed:affiliation
Structural and Computational Biology Unit, European Molecular Biology Laboratory, Meyerhofstrasse 1, 69117 Heidelberg, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't