Literature DB >> 1406644

Purification of splicing factor SF1, a heat-stable protein that functions in the assembly of a presplicing complex.

A Krämer1.   

Abstract

Splicing factor SF1 represents one of the proteins that function early in the splicing of nuclear pre-mRNA in the formation of a presplicing complex. SF1 was purified to homogeneity from HeLa cell nuclear extracts by column chromatography. It consists of a single polypeptide of 75 kDa and is distinct from other protein factors that function early in spliceosome assembly. SF1 activity is completely resistant to temperatures of up to 100 degrees C. The purified protein does not appear to be associated with RNA-binding, RNA-annealing, or ATPase activity.

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Year:  1992        PMID： 1406644      PMCID： PMC360381          DOI： 10.1128/mcb.12.10.4545-4552.1992

Source DB:  PubMed          Journal:  Mol Cell Biol        ISSN： 0270-7306            Impact factor:   4.272


  44 in total

1.  Identification, purification, and biochemical characterization of U2 small nuclear ribonucleoprotein auxiliary factor.

Authors:  P D Zamore; M R Green
Journal:  Proc Natl Acad Sci U S A       Date:  1989-12       Impact factor: 11.205

2.  Interactions between small nuclear ribonucleoprotein particles in formation of spliceosomes.

Authors:  M M Konarska; P A Sharp
Journal:  Cell       Date:  1987-06-19       Impact factor: 41.582

3.  A protein associated with small nuclear ribonucleoprotein particles recognizes the 3' splice site of premessenger RNA.

Authors:  V Gerke; J A Steitz
Journal:  Cell       Date:  1986-12-26       Impact factor: 41.582

4.  Separation of multiple components of HeLa cell nuclear extracts required for pre-messenger RNA splicing.

Authors:  A Krämer; M Frick; W Keller
Journal:  J Biol Chem       Date:  1987-12-25       Impact factor: 5.157

5.  A factor, U2AF, is required for U2 snRNP binding and splicing complex assembly.

Authors:  B Ruskin; P D Zamore; M R Green
Journal:  Cell       Date:  1988-01-29       Impact factor: 41.582

6.  Spliceosome assembly in yeast.

Authors:  S C Cheng; J Abelson
Journal:  Genes Dev       Date:  1987-11       Impact factor: 11.361

7.  An early hierarchic role of U1 small nuclear ribonucleoprotein in spliceosome assembly.

Authors:  S W Ruby; J Abelson
Journal:  Science       Date:  1988-11-18       Impact factor: 47.728

8.  Purification of an octamer sequence (ATGCAAAT)-binding protein from human B cells.

Authors:  J Y Wang; K Nishiyama; K Araki; D Kitamura; T Watanabe
Journal:  Nucleic Acids Res       Date:  1987-12-23       Impact factor: 16.971

9.  Identification and purification of a 62,000-dalton protein that binds specifically to the polypyrimidine tract of introns.

Authors:  M A García-Blanco; S F Jamison; P A Sharp
Journal:  Genes Dev       Date:  1989-12       Impact factor: 11.361

10.  An ordered pathway of snRNP binding during mammalian pre-mRNA splicing complex assembly.

Authors:  A Bindereif; M R Green
Journal:  EMBO J       Date:  1987-08       Impact factor: 11.598
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  47 in total

1.  The tetranucleotide UCAY directs the specific recognition of RNA by the Nova K-homology 3 domain.

Authors:  K B Jensen; K Musunuru; H A Lewis; S K Burley; R B Darnell
Journal:  Proc Natl Acad Sci U S A       Date:  2000-05-23       Impact factor: 11.205

2.  The transcription elongation factor CA150 interacts with RNA polymerase II and the pre-mRNA splicing factor SF1.

Authors:  A C Goldstrohm; T R Albrecht; C Suñé; M T Bedford; M A Garcia-Blanco
Journal:  Mol Cell Biol       Date:  2001-11       Impact factor: 4.272

3.  Large-scale proteomic analysis of the human spliceosome.

Authors:  Juri Rappsilber; Ursula Ryder; Angus I Lamond; Matthias Mann
Journal:  Genome Res       Date:  2002-08       Impact factor: 9.043

4.  The WW domain-containing proteins interact with the early spliceosome and participate in pre-mRNA splicing in vivo.

Authors:  Kai-Ti Lin; Ruei-Min Lu; Woan-Yuh Tarn
Journal:  Mol Cell Biol       Date:  2004-10       Impact factor: 4.272

5.  Composition and three-dimensional EM structure of double affinity-purified, human prespliceosomal A complexes.

Authors:  Nastaran Behzadnia; Monika M Golas; Klaus Hartmuth; Bjoern Sander; Berthold Kastner; Jochen Deckert; Prakash Dube; Cindy L Will; Henning Urlaub; Holger Stark; Reinhard Lührmann
Journal:  EMBO J       Date:  2007-03-01       Impact factor: 11.598

6.  Recognition of RNA branch point sequences by the KH domain of splicing factor 1 (mammalian branch point binding protein) in a splicing factor complex.

Authors:  H Peled-Zehavi; J A Berglund; M Rosbash; A D Frankel
Journal:  Mol Cell Biol       Date:  2001-08       Impact factor: 4.272

7.  CUS2, a yeast homolog of human Tat-SF1, rescues function of misfolded U2 through an unusual RNA recognition motif.

Authors:  D Yan; R Perriman; H Igel; K J Howe; M Neville; M Ares
Journal:  Mol Cell Biol       Date:  1998-09       Impact factor: 4.272

8.  A role for SRp54 during intron bridging of small introns with pyrimidine tracts upstream of the branch point.

Authors:  C F Kennedy; A Krämer; S M Berget
Journal:  Mol Cell Biol       Date:  1998-09       Impact factor: 4.272

9.  The KH domain of the branchpoint sequence binding protein determines specificity for the pre-mRNA branchpoint sequence.

Authors:  J A Berglund; M L Fleming; M Rosbash
Journal:  RNA       Date:  1998-08       Impact factor: 4.942

10.  Quaking and PTB control overlapping splicing regulatory networks during muscle cell differentiation.

Authors:  Megan P Hall; Roland J Nagel; W Samuel Fagg; Lily Shiue; Melissa S Cline; Rhonda J Perriman; John Paul Donohue; Manuel Ares
Journal:  RNA       Date:  2013-03-22       Impact factor: 4.942
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