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Human immunodeficiency virus type 1 hnRNP A/B-dependent exonic splicing silencer ESSV antagonizes binding of U2AF65 to viral polypyrimidine tracts.
Mol Cell Biol. 2003 Dec; 23(23):8762-72.MC

Abstract

Human immunodeficiency virus type 1 (HIV-1) exonic splicing silencers (ESSs) inhibit production of certain spliced viral RNAs by repressing alternative splicing of the viral precursor RNA. Several HIV-1 ESSs interfere with spliceosome assembly by binding cellular hnRNP A/B proteins. Here, we have further characterized the mechanism of splicing repression using a representative HIV-1 hnRNP A/B-dependent ESS, ESSV, which regulates splicing at the vpr 3' splice site. We show that hnRNP A/B proteins bound to ESSV are necessary to inhibit E complex assembly by competing with the binding of U2AF65 to the polypyrimidine tracts of repressed 3' splice sites. We further show evidence suggesting that U1 snRNP binds the 5' splice site despite an almost complete block of splicing by ESSV. Possible splicing-independent functions of U1 snRNP-5' splice site interactions during virus replication are discussed.

Authors+Show Affiliations

Program in Molecular Biology, University of Iowa, Iowa City, Iowa 52242, USA.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.

Language

eng

PubMed ID

14612416

Citation

Domsic, Jeffrey K., et al. "Human Immunodeficiency Virus Type 1 hnRNP A/B-dependent Exonic Splicing Silencer ESSV Antagonizes Binding of U2AF65 to Viral Polypyrimidine Tracts." Molecular and Cellular Biology, vol. 23, no. 23, 2003, pp. 8762-72.
Domsic JK, Wang Y, Mayeda A, et al. Human immunodeficiency virus type 1 hnRNP A/B-dependent exonic splicing silencer ESSV antagonizes binding of U2AF65 to viral polypyrimidine tracts. Mol Cell Biol. 2003;23(23):8762-72.
Domsic, J. K., Wang, Y., Mayeda, A., Krainer, A. R., & Stoltzfus, C. M. (2003). Human immunodeficiency virus type 1 hnRNP A/B-dependent exonic splicing silencer ESSV antagonizes binding of U2AF65 to viral polypyrimidine tracts. Molecular and Cellular Biology, 23(23), 8762-72.
Domsic JK, et al. Human Immunodeficiency Virus Type 1 hnRNP A/B-dependent Exonic Splicing Silencer ESSV Antagonizes Binding of U2AF65 to Viral Polypyrimidine Tracts. Mol Cell Biol. 2003;23(23):8762-72. PubMed PMID: 14612416.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Human immunodeficiency virus type 1 hnRNP A/B-dependent exonic splicing silencer ESSV antagonizes binding of U2AF65 to viral polypyrimidine tracts. AU - Domsic,Jeffrey K, AU - Wang,Yibin, AU - Mayeda,Akila, AU - Krainer,Adrian R, AU - Stoltzfus,C Martin, PY - 2003/11/13/pubmed PY - 2003/12/17/medline PY - 2003/11/13/entrez SP - 8762 EP - 72 JF - Molecular and cellular biology JO - Mol Cell Biol VL - 23 IS - 23 N2 - Human immunodeficiency virus type 1 (HIV-1) exonic splicing silencers (ESSs) inhibit production of certain spliced viral RNAs by repressing alternative splicing of the viral precursor RNA. Several HIV-1 ESSs interfere with spliceosome assembly by binding cellular hnRNP A/B proteins. Here, we have further characterized the mechanism of splicing repression using a representative HIV-1 hnRNP A/B-dependent ESS, ESSV, which regulates splicing at the vpr 3' splice site. We show that hnRNP A/B proteins bound to ESSV are necessary to inhibit E complex assembly by competing with the binding of U2AF65 to the polypyrimidine tracts of repressed 3' splice sites. We further show evidence suggesting that U1 snRNP binds the 5' splice site despite an almost complete block of splicing by ESSV. Possible splicing-independent functions of U1 snRNP-5' splice site interactions during virus replication are discussed. SN - 0270-7306 UR - https://www.unboundmedicine.com/medline/citation/14612416/Human_immunodeficiency_virus_type_1_hnRNP_A/B_dependent_exonic_splicing_silencer_ESSV_antagonizes_binding_of_U2AF65_to_viral_polypyrimidine_tracts_ L2 - http://mcb.asm.org/cgi/pmidlookup?view=long&pmid=14612416 DB - PRIME DP - Unbound Medicine ER -