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A cellular protein, hnRNP H, binds to the negative regulator of splicing element from Rous sarcoma virus.
J Biol Chem. 2000 Oct 13; 275(41):32371-8.JB

Abstract

Incomplete RNA splicing is a key feature of the retroviral life cycle. This is in contrast to the processing of most cellular pre-mRNAs, which are usually spliced to completion. In Rous sarcoma virus, splicing control is achieved in part through a cis-acting RNA element termed the negative regulator of splicing (NRS). The NRS is functionally divided into two parts termed NRS5' and NRS3', which bind a number of splicing factors. The U1 and U11 small nuclear ribonucleoproteins interact with sequences in NRS3', whereas NRS5' binds several proteins including members of the SR [corrected] family of proteins. Among the proteins that specifically bind NRS5' is a previously unidentified 55-kDa protein (p55). In this report we describe the isolation and identification of p55. The p55 binding site was localized by UV cross-linking to a 31-nucleotide segment, and a protein that binds specifically to it was isolated by RNA affinity selection and identified by mass spectrometry as hnRNP H. Antibodies against hnRNP H immunoprecipitated cross-linked p55 and induced a supershift of a p55-containing complex formed in HeLa nuclear extract. Furthermore, UV cross-linking and electrophoretic mobility shift assays indicated that recombinant hnRNP H specifically interacts with the p55 binding site, confirming that hnRNP H is p55. The possible roles of hnRNP H in NRS function are discussed.

Authors+Show Affiliations

Department of Microbiology and Molecular Genetics, Medical College of Wisconsin, Milwaukee, Wisconsin 53226, USA.No affiliation info available

Pub Type(s)

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

Language

eng

PubMed ID

10934202

Citation

Fogel, B L., and M T. McNally. "A Cellular Protein, hnRNP H, Binds to the Negative Regulator of Splicing Element From Rous Sarcoma Virus." The Journal of Biological Chemistry, vol. 275, no. 41, 2000, pp. 32371-8.
Fogel BL, McNally MT. A cellular protein, hnRNP H, binds to the negative regulator of splicing element from Rous sarcoma virus. J Biol Chem. 2000;275(41):32371-8.
Fogel, B. L., & McNally, M. T. (2000). A cellular protein, hnRNP H, binds to the negative regulator of splicing element from Rous sarcoma virus. The Journal of Biological Chemistry, 275(41), 32371-8.
Fogel BL, McNally MT. A Cellular Protein, hnRNP H, Binds to the Negative Regulator of Splicing Element From Rous Sarcoma Virus. J Biol Chem. 2000 Oct 13;275(41):32371-8. PubMed PMID: 10934202.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - A cellular protein, hnRNP H, binds to the negative regulator of splicing element from Rous sarcoma virus. AU - Fogel,B L, AU - McNally,M T, PY - 2000/8/10/pubmed PY - 2001/2/28/medline PY - 2000/8/10/entrez SP - 32371 EP - 8 JF - The Journal of biological chemistry JO - J Biol Chem VL - 275 IS - 41 N2 - Incomplete RNA splicing is a key feature of the retroviral life cycle. This is in contrast to the processing of most cellular pre-mRNAs, which are usually spliced to completion. In Rous sarcoma virus, splicing control is achieved in part through a cis-acting RNA element termed the negative regulator of splicing (NRS). The NRS is functionally divided into two parts termed NRS5' and NRS3', which bind a number of splicing factors. The U1 and U11 small nuclear ribonucleoproteins interact with sequences in NRS3', whereas NRS5' binds several proteins including members of the SR [corrected] family of proteins. Among the proteins that specifically bind NRS5' is a previously unidentified 55-kDa protein (p55). In this report we describe the isolation and identification of p55. The p55 binding site was localized by UV cross-linking to a 31-nucleotide segment, and a protein that binds specifically to it was isolated by RNA affinity selection and identified by mass spectrometry as hnRNP H. Antibodies against hnRNP H immunoprecipitated cross-linked p55 and induced a supershift of a p55-containing complex formed in HeLa nuclear extract. Furthermore, UV cross-linking and electrophoretic mobility shift assays indicated that recombinant hnRNP H specifically interacts with the p55 binding site, confirming that hnRNP H is p55. The possible roles of hnRNP H in NRS function are discussed. SN - 0021-9258 UR - https://www.unboundmedicine.com/medline/citation/10934202/A_cellular_protein_hnRNP_H_binds_to_the_negative_regulator_of_splicing_element_from_Rous_sarcoma_virus_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0021-9258(20)89329-6 DB - PRIME DP - Unbound Medicine ER -