A proteomic approach to the identification of heterogeneous nuclear ribonucleoproteins as a new family of poly(ADP-ribose)-binding proteins - PubMed (original) (raw)

A proteomic approach to the identification of heterogeneous nuclear ribonucleoproteins as a new family of poly(ADP-ribose)-binding proteins

Jean-Philippe Gagné et al. Biochem J. 2003.

Abstract

A new class of poly(ADP-ribose) (pADPr)-binding proteins, heterogeneous nuclear ribonucleoproteins (hnRNPs), has been identified by a proteomic approach using matrix-assisted laser-desorption-ionization time-of-flight ('MALDI-TOF') MS. Liquid-phase isoelectric focusing with a Rotofor cell (Bio-Rad) allowed pre-fractionation of proteins extracted from HeLa cells. Rotofor protein fractions were further separated by SDS/PAGE and then transferred to a PVDF membrane. pADPr-binding proteins were analysed by autoradiography of the protein blot after incubation with (32)P-labelled automodified pADPr polymerase-1 (PARP-1). Peptide mass fingerprinting of selected bands identified the most abundant pADPr-binding proteins as hnRNPs, a family of proteins that bind pre-mRNA into functional complexes involved in mRNA maturation and transport to the cytoplasm. Sequence homology database searching against a previously reported pADPr-binding sequence motif revealed that the hnRNPs contain a putative pADPr-binding sequence pattern [Pleschke, Kleczkowska, Strohm and Althaus (2000) J. Biol. Chem. 275, 40974-40980]. pADPr-binding assays performed with synthetic peptides by the dot-blot technique and with nitrocellulose-transferred recombinant hnRNPs confirmed the pADPr-binding protein identification and the specificity of the interaction. These results could establish a link between increased levels of pADPr in DNA damaged cells and the modified protein expression pattern resulting from altered mRNA trafficking.

PubMed Disclaimer

Cited by

New facets in the regulation of gene expression by ADP-ribosylation and poly(ADP-ribose) polymerases.
Ryu KW, Kim DS, Kraus WL. Ryu KW, et al. Chem Rev. 2015 Mar 25;115(6):2453-81. doi: 10.1021/cr5004248. Epub 2015 Jan 9. Chem Rev. 2015. PMID: 25575290 Free PMC article. Review. No abstract available.
Poly(ADP-ribosyl)ation of heterogeneous nuclear ribonucleoproteins modulates splicing.
Ji Y, Tulin AV. Ji Y, et al. Nucleic Acids Res. 2009 Jun;37(11):3501-13. doi: 10.1093/nar/gkp218. Epub 2009 Apr 3. Nucleic Acids Res. 2009. PMID: 19346337 Free PMC article.
Functional roles of ADP-ribosylation writers, readers and erasers.
Li P, Lei Y, Qi J, Liu W, Yao K. Li P, et al. Front Cell Dev Biol. 2022 Aug 11;10:941356. doi: 10.3389/fcell.2022.941356. eCollection 2022. Front Cell Dev Biol. 2022. PMID: 36035988 Free PMC article. Review.
Nuclear ADP-ribosylation reactions in mammalian cells: where are we today and where are we going?
Hassa PO, Haenni SS, Elser M, Hottiger MO. Hassa PO, et al. Microbiol Mol Biol Rev. 2006 Sep;70(3):789-829. doi: 10.1128/MMBR.00040-05. Microbiol Mol Biol Rev. 2006. PMID: 16959969 Free PMC article. Review.
Potential therapeutic approaches for modulating expression and accumulation of defective lamin A in laminopathies and age-related diseases.
Zhavoronkov A, Smit-McBride Z, Guinan KJ, Litovchenko M, Moskalev A. Zhavoronkov A, et al. J Mol Med (Berl). 2012 Dec;90(12):1361-89. doi: 10.1007/s00109-012-0962-4. Epub 2012 Oct 23. J Mol Med (Berl). 2012. PMID: 23090008 Free PMC article. Review.

References

1. J Biol Chem. 1993 Aug 25;268(24):17662-4 - PubMed
1. J Mol Biol. 1993 Feb 20;229(4):873-89 - PubMed
1. Biochim Biophys Acta. 1994 Oct 18;1219(2):342-50 - PubMed
1. EMBO J. 1994 Nov 15;13(22):5483-95 - PubMed
1. Biochem Biophys Res Commun. 1994 Oct 28;204(2):772-9 - PubMed

A proteomic approach to the identification of heterogeneous nuclear ribonucleoproteins as a new family of poly(ADP-ribose)-binding proteins - PubMed (original) (raw)