scholarly journals Serine/Arginine-Rich Splicing Factor 1

2020 ◽  
Author(s):  
Keyword(s):  
Splicing Factor ◽  
Splicing Factor 1

scholarly journals Splicing factor 1 modulates dietary restriction and TORC1 pathway longevity in C. elegans

Nature ◽  
2016 ◽  
Vol 541 (7635) ◽  
pp. 102-106 ◽  
Author(s):  
Caroline Heintz ◽  
Thomas K. Doktor ◽  
Anne Lanjuin ◽  
Caroline C. Escoubas ◽  
Yue Zhang ◽  
...  
Keyword(s):  
Dietary Restriction ◽  
Splicing Factor ◽  
C Elegans ◽  
Splicing Factor 1

scholarly journals Competition between a noncoding exon and introns: Gomafu contains tandem UACUAAC repeats and associates with splicing factor-1

2011 ◽  
Vol 16 (5) ◽  
pp. 479-490 ◽  
Author(s):  
Hitomi Tsuiji ◽  
Rei Yoshimoto ◽  
Yuko Hasegawa ◽  
Masaaki Furuno ◽  
Minoru Yoshida ◽  
...  
Keyword(s):  
Splicing Factor ◽  
Noncoding Exon ◽  
Splicing Factor 1

scholarly journals Recognition of RNA Branch Point Sequences by the KH Domain of Splicing Factor 1 (Mammalian Branch Point Binding Protein) in a Splicing Factor Complex

2001 ◽  
Vol 21 (15) ◽  
pp. 5232-5241 ◽  
Author(s):  
Hadas Peled-Zehavi ◽  
J. Andrew Berglund ◽  
Michael Rosbash ◽  
Alan D. Frankel
Keyword(s):  
Branch Point ◽  
Fusion Proteins ◽  
Rna Binding ◽  
Binding Protein ◽  
Splicing Factor ◽  
Splice Sites ◽  
Reporter System ◽  
Kh Domain ◽  
Tat Fusion Proteins ◽  
Splicing Factor 1

ABSTRACT Mammalian splicing factor 1 (SF1; also mammalian branch point binding protein [mBBP]; hereafter SF1/mBBP) specifically recognizes the seven-nucleotide branch point sequence (BPS) located at 3′ splice sites and participates in the assembly of early spliceosomal complexes. SF1/mBBP utilizes a “maxi-K homology” (maxi-KH) domain for recognition of the single-stranded BPS and requires a cooperative interaction with splicing factor U2AF65 bound to an adjacent polypyrimidine tract (PPT) for high-affinity binding. To investigate how the KH domain of SF1/mBBP recognizes the BPS in conjunction with U2AF and possibly other proteins, we constructed a transcriptional reporter system utilizing human immunodeficiency virus type 1 Tat fusion proteins and examined the RNA-binding specificity of the complex using KH domain and RNA-binding site mutants. We first established that SF1/mBBP and U2AF cooperatively assemble in our reporter system at RNA sites composed of the BPS, PPT, and AG dinucleotide found at 3′ splice sites, with endogenous proteins assembled along with the Tat fusions. We next found that the activities of the Tat fusion proteins on different BPS variants correlated well with the known splicing efficiencies of the variants, supporting a model in which the SF1/mBBP-BPS interaction helps determine splicing efficiency prior to the U2 snRNP-BPS interaction. Finally, the likely RNA-binding surface of the maxi-KH domain was identified by mutagenesis and appears similar to that used by “simple” KH domains, involving residues from two putative α helices, a highly conserved loop, and parts of a β sheet. Using a homology model constructed from the cocrystal structure of a Nova KH domain-RNA complex (Lewis et al., Cell 100:323–332, 2000), we propose a plausible arrangement for SF1/mBBP-U2AF complexes assembled at 3′ splice sites.

scholarly journals Splicing Factor 1 in the Pocket

Structure ◽  
2003 ◽  
Vol 11 (5) ◽  
pp. 481-482 ◽  
Author(s):  
Gabriele Varani ◽  
Andres Ramos
Keyword(s):  
Splicing Factor ◽  
Splicing Factor 1

scholarly journals A Role for SRp54 during Intron Bridging of Small Introns with Pyrimidine Tracts Upstream of the Branch Point

1998 ◽  
Vol 18 (9) ◽  
pp. 5425-5434 ◽  
Author(s):  
Catharine F. Kennedy ◽  
Angela Krämer ◽  
Susan M. Berget
Keyword(s):  
Binding Site ◽  
Branch Point ◽  
Splice Site ◽  
Early Recognition ◽  
Splicing Factor ◽  
Splicing Factors ◽  
Sr Protein ◽  
U2 Snrnp ◽  
Auxiliary Factor ◽  
Splicing Factor 1

ABSTRACT One of the earliest steps in pre-mRNA recognition involves binding of the splicing factor U2 snRNP auxiliary factor (U2AF or MUD2 inSaccharomyces cerevisiae) to the 3′ splice site region. U2AF interacts with a number of other proteins, including members of the serine/arginine (SR) family of splicing factors as well as splicing factor 1 (SF1 or branch point bridging protein in S. cerevisiae), thereby participating in bridging either exons or introns. In vertebrates, the binding site for U2AF is the pyrimidine tract located between the branch point and 3′ splice site. Many small introns, especially those in nonvertebrates, lack a classical 3′ pyrimidine tract. Here we show that a 59-nucleotide Drosophila melanogaster intron contains C-rich pyrimidine tracts between the 5′ splice site and branch point that are needed for maximal binding of both U1 snRNPs and U2 snRNPs to the 5′ and 3′ splice site, respectively, suggesting that the tracts are the binding site for an intron bridging factor. The tracts are shown to bind both U2AF and the SR protein SRp54 but not SF1. Addition of a strong 3′ pyrimidine tract downstream of the branch point increases binding of SF1, but in this context, the upstream pyrimidine tracts are inhibitory. We suggest that U2AF- and/or SRp54-mediated intron bridging may be an alternative early recognition mode to SF1-directed bridging for small introns, suggesting gene-specific early spliceosome assembly.

scholarly journals A Conserved DrosophilaTransportin-Serine/Arginine-rich (SR) Protein Permits Nuclear Import ofDrosophila SR Protein Splicing Factors and Their Antagonist Repressor Splicing Factor 1

2002 ◽  
Vol 13 (7) ◽  
pp. 2436-2447 ◽  
Author(s):  
Eric Allemand ◽  
Svetlana Dokudovskaya ◽  
Rémy Bordonné ◽  
Jamal Tazi
Keyword(s):  
Nuclear Import ◽  
Direct Interaction ◽  
Sr Proteins ◽  
Splicing Factor ◽  
Nuclear Speckles ◽  
Sr Protein ◽  
Nuclear Factors ◽  
Localization Signal ◽  
Import Receptors ◽  
Splicing Factor 1

Members of the highly conserved serine/arginine-rich (SR) protein family are nuclear factors involved in splicing of metazoan mRNA precursors. In mammals, two nuclear import receptors, transportin (TRN)-SR1 and TRN-SR2, are responsible for targeting SR proteins to the nucleus. Distinctive features in the nuclear localization signal between Drosophila and mammalian SR proteins prompted us to examine the mechanism by whichDrosophila SR proteins and their antagonist repressor splicing factor 1 (RSF1) are imported into nucleus. Herein, we report the identification and characterization of a Drosophilaimportin β-family protein (dTRN-SR), homologous to TRN-SR2, that specifically interacts with both SR proteins and RSF1. dTRN-SR has a broad localization in the cytoplasm and the nucleus, whereas an N-terminal deletion mutant colocalizes with SR proteins in nuclear speckles. Far Western experiments established that the RS domain of SR proteins and the GRS domain of RSF1 are required for the direct interaction with dTRN-SR, an interaction that can be modulated by phosphorylation. Using the yeast model system in which nuclear import of Drosophila SR proteins and RSF1 is impaired, we demonstrate that complementation with dTRN-SR is sufficient to target these proteins to the nucleus. Together, the results imply that the mechanism by which SR proteins are imported to the nucleus is conserved between Drosophila and humans.

scholarly journals Erratum: Corrigendum: Splicing factor 1 modulates dietary restriction and TORC1 pathway longevity in C. elegans

Nature ◽  
2017 ◽  
Vol 547 (7664) ◽  
pp. 476-476 ◽  
Author(s):  
Caroline Heintz ◽  
Thomas K. Doktor ◽  
Anne Lanjuin ◽  
Caroline C. Escoubas ◽  
Yue Zhang ◽  
...  
Keyword(s):  
Dietary Restriction ◽  
Splicing Factor ◽  
C Elegans ◽  
Splicing Factor 1
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