SF2/ASF binds to a splicing enhancer in the third HIV-1 tat exon and stimulates U2AF binding independently of the RS domain

Journal of Molecular Biology

Volumn 312, Issue 4, 2001, Pages 649-662

  Tange, Thomas Ø ^a   Kjems, Jørgen ^a  

^a AARHUS UNIVERSITY   (Denmark)

Author keywords

Exon splicing enhancer; Exon splicing silencer; RNA splicing; SF2 ASF; U2AF

Indexed keywords

PROTEIN; PROTEIN ASF; PROTEIN SF 2; TRANSACTIVATOR PROTEIN; UNCLASSIFIED DRUG;

ARTICLE; EXON; HUMAN; HUMAN CELL; HUMAN IMMUNODEFICIENCY VIRUS 1; INTRON; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN CROSS LINKING; PROTEIN EXPRESSION; PROTEIN PURIFICATION; RNA SPLICING;

EID: 0035965130     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2001.4971     Document Type: Article

References (69)

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25. General splicing factor SF2/ASF promotes alternative splicing by binding to an exonic splicing enhancer
26. A splicing enhancer in the human fibronectin alternate ED1 exon interacts with SR proteins and stimulates U2 snRNP binding
27. A subset of SR proteins activates splicing of the cardiac troponin T alternative exon by direct interactions with an exonic enhancer
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31. Intrinsic U2AF binding is modulated by exon enhancer signals in parallel with changes in splicing activity
32. The splicing factor U2AF35 mediates critical protein-protein interactions in constitutive and enhancer-dependent splicing
33. Pre-mRNA splicing of IgM exons M1 and M2 is directed by a juxtaposed splicing enhancer and inhibitor
34. The SRm160/300 splicing coactivator is required for exon-enhancer function
35. Distinct factor requirements for exonic splicing enhancer function and binding of U2AF to the polypyrimidine tract
36. A novel bipartite splicing enhancer modulates the differential processing of the human fibronectin EDA exon
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38. Exon and intron sequences, respectively, repress and activate splicing of a fibroblast growth factor receptor 2 alternative exon
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40. Presence of exon splicing silencers within human immunodeficiency virus type 1 tat exon 2 and tat-rev exon 3: Evidence for inhibition mediated by cellular factors
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50. Splicing efficiency of human immunodeficiency virus type 1 tat RNA is determined by both a suboptimal 3′ splice site and a 10 nucleotide exon splicing silencer element located within tat exon 2
51. The tat/rev intron of human immunodeficiency virus type 1 is inefficiently spliced because of suboptimal signals in the 3′ splice site
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53. Substrate specificities of SR proteins in constitutive splicing are determined by their RNA recognition motifs and composite pre-mRNA exonic elements
54. The sequence complementarity between HIV-1 5′ splice site SD4 and U1 snRNA determines the steady-state level of an unstable env pre-mRNA
55. The exon splicing silencer in human immunodeficiency virus type 1 Tat exon 3 is bipartite and acts early in spliceosome assembly
56. Synergistic interactions between two distinct elements of a regulated splicing enhancer
57. Identification of functional exonic splicing enhancer motifs recognized by individual SR proteins
58. The human splicing factors ASF/SF2 and SC35 possess distinct, functionally significant RNA binding specificities
59. Human Tra2 proteins are sequence-specific activators of pre-mRNA splicing
60. Assembly of specific SR protein complexes on distinct regulatory elements of the Drosophila doublesex splicing enhancer
61. Functional analysis of pre-mRNA splicing factor SF2/ASF structural domains
62. Functional domains of the human splicing factor ASF/SF2
63. RNA splicing specificity determined by the coordinated action of RNA recognition motifs in SR proteins
64. Genetic analysis of the SR protein ASF/SF2: Interchangeability of RS domains and negative control of splicing
65. Pre-mRNA splicing in the absence of an SR protein RS domain
66. The spliceosome assembly pathway in mammalian extracts
67. Primary structure of the human splicing factor ASF reveals similarities with Drosophila regulators
68. Evidence for substrate-specific requirement of the splicing factor U2AF(35) and for its function after polypyrimidine tract recognition by U2AF(65)