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PCBP2  -  poly(rC) binding protein 2

Homo sapiens

Synonyms: Alpha-CP2, HNRNPE2, HNRPE2, Heterogeneous nuclear ribonucleoprotein E2, Poly(rC)-binding protein 2, ...
 
 
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Disease relevance of PCBP2

  • PCBP1 and PCBP2 specifically interact with both the 5'-element known as the cloverleaf structure and the large stem-loop IV RNA of the poliovirus 5'-untranslated region [1].
  • PCBP2, as well as a related protein, PCBP1, was over-expressed in Escherichia coli after cloning the cDNAs into an expression plasmid to produce a histidine-tagged fusion protein [2].
  • We found that SRp20 interacts with the cellular RNA-binding protein, PCBP2, a protein that binds to IRES sequences within the genomic RNAs of certain picornaviruses and is required for viral translation [3].
  • We have examined the requirement of the cellular protein poly(rC) binding protein 2 (PCBP2) for hepatitis A virus (HAV) RNA translation [4].
  • Upon depletion of PCBP2, these extracts possessed a significantly diminished capacity to translate reporter RNAs containing the type I IRES elements of poliovirus, coxsackievirus, or human rhinovirus linked to luciferase; however, the addition of recombinant PCBP2 could reconstitute translation [5].
 

High impact information on PCBP2

  • BCR-ABL suppresses C/EBPalpha expression through inhibitory action of hnRNP E2 [6].
  • In contrast, the other ESS1-binding proteins, PTB and hnRNP E2, do not discriminate between wild-type and mutant ESS1 in binding studies, and do not specifically alter ESS1-dependent splicing in vitro [7].
  • Epitope-tagged recombinant alpha CP-1 and alpha CP-2 expressed in cells are each incorporated into the alpha-complex [8].
  • The sequence obtained matched that of poly(rC) binding protein 2 (PCBP2), previously identified as an RNA binding protein from human cells [2].
  • Stem-loop IV RNA containing a three nucleotide insertion that abrogates translation activity and virus viability was unable to bind PCBP2 [2].
 

Chemical compound and disease context of PCBP2

 

Biological context of PCBP2

  • One host protein that plays a role in both translation initiation and viral RNA synthesis is poly(rC) binding protein 2 (PCBP2) [10].
  • To reveal the molecular basis of poly(C) sequence recognition, we have determined the crystal structure, at 1.7-A resolution, of PCBP2 KH1 in complex with a 7-nucleotide DNA sequence (5'-AACCCTA-3') corresponding to one repeat of the human C-rich strand telomeric DNA [11].
  • The co-crystal structure also reveals a protein-protein dimerization interface of PCBP2 KH1 located on the opposite side of the protein from the DNA binding groove [11].
  • Interaction of PCBP2 KH1 with the C-rich strand of human telomeric DNA suggests that PCBPs may participate in mechanisms involved in the regulation of telomere/telomerase functions [11].
  • The two RNA variants differ at only one position (C vs U) within a six-nucleotide asymmetric internal loop sequence that is the binding site for the PCBP2 KH1 domain [12].
 

Anatomical context of PCBP2

  • For picornavirus RNAs containing type I internal ribosome entry site (IRES) elements, PCBP2 binds the major stem-loop structure (stem-loop IV) in the IRES and is essential for translation initiation [10].
  • HeLa cell extracts subjected to stem-loop IV RNA affinity chromatography were depleted of all detectable PCBP2 [13].
  • Initiation of viral translation in Xenopus oocytes is strongly inhibited by co-injection of specific antibodies directed against PCBP1 or PCBP2, indicating that the poly(rC) binding proteins may facilitate this process [14].
  • We prepared a PCBP2-immunodepleted rabbit reticulocyte lysate with an anti-PCBP2 antibody [15].
 

Associations of PCBP2 with chemical compounds

  • This suggests that the hnRNPs could fall into two groups: one group, including hnRNP A1 and C1, involved in hnRNP core complex formation and another group, including hnRNP E2, I, K, and L, involved in a variety of RNA-related biological processes [16].
 

Physical interactions of PCBP2

 

Other interactions of PCBP2

  • The poly(rC)-binding proteins (PCBP1 and PCBP2) are RNA-binding proteins whose RNA recognition motifs are composed of three K homology (KH) domains [1].
  • Studies on PV1 have shown that specific recognition of loop B by the first KH (hnRNP K homology) domain of cellular poly(rC)-binding protein 2 (PCBP2) is essential for efficient translation of the viral mRNA [12].
  • We have previously purified four factors (alpha-IRP, alpha-CP1, alpha-CP2, and NF-E1) that interact with the promoter of the alpha-globin gene [18].
  • Comparison of the amino acid sequence of LBP-1 with entries in the available protein data bases revealed the identity of LBP-1c to alpha-CP2, an alpha-globin transcription factor [19].
  • Specific regulatory regions were identified in the gamma- and beta-globin gene promoters to which new binding of transcription factors, including alpha CP2 (an activator of gamma globin) occur during therapy solely in the butyrate-responsive patients [20].
 

Analytical, diagnostic and therapeutic context of PCBP2

  • Competition RNA mobility shift assays showed that the 5'NCR of HAV RNA competed for binding of PCBP2 with a probe representing stem-loop IV of the PV 5'NCR [4].

References

  1. The N-terminal K homology domain of the poly(rC)-binding protein is a major determinant for binding to the poliovirus 5'-untranslated region and acts as an inhibitor of viral translation. Silvera, D., Gamarnik, A.V., Andino, R. J. Biol. Chem. (1999) [Pubmed]
  2. Poly(rC) binding protein 2 binds to stem-loop IV of the poliovirus RNA 5' noncoding region: identification by automated liquid chromatography-tandem mass spectrometry. Blyn, L.B., Swiderek, K.M., Richards, O., Stahl, D.C., Semler, B.L., Ehrenfeld, E. Proc. Natl. Acad. Sci. U.S.A. (1996) [Pubmed]
  3. A nucleo-cytoplasmic SR protein functions in viral IRES-mediated translation initiation. Bedard, K.M., Daijogo, S., Semler, B.L. EMBO J. (2007) [Pubmed]
  4. Interaction of poly(rC) binding protein 2 with the 5' noncoding region of hepatitis A virus RNA and its effects on translation. Graff, J., Cha, J., Blyn, L.B., Ehrenfeld, E. J. Virol. (1998) [Pubmed]
  5. Differential utilization of poly(rC) binding protein 2 in translation directed by picornavirus IRES elements. Walter, B.L., Nguyen, J.H., Ehrenfeld, E., Semler, B.L. RNA (1999) [Pubmed]
  6. BCR-ABL suppresses C/EBPalpha expression through inhibitory action of hnRNP E2. Perrotti, D., Cesi, V., Trotta, R., Guerzoni, C., Santilli, G., Campbell, K., Iervolino, A., Condorelli, F., Gambacorti-Passerini, C., Caligiuri, M.A., Calabretta, B. Nat. Genet. (2002) [Pubmed]
  7. HnRNP L represses exon splicing via a regulated exonic splicing silencer. Rothrock, C.R., House, A.E., Lynch, K.W. EMBO J. (2005) [Pubmed]
  8. Identification of two KH domain proteins in the alpha-globin mRNP stability complex. Kiledjian, M., Wang, X., Liebhaber, S.A. EMBO J. (1995) [Pubmed]
  9. Selection and cloning of poly(rC)-binding protein 2 and Raf kinase inhibitor protein RNA activators of 2',5'-oligoadenylate synthetase from prostate cancer cells. Molinaro, R.J., Jha, B.K., Malathi, K., Varambally, S., Chinnaiyan, A.M., Silverman, R.H. Nucleic Acids Res. (2006) [Pubmed]
  10. Distinct poly(rC) binding protein KH domain determinants for poliovirus translation initiation and viral RNA replication. Walter, B.L., Parsley, T.B., Ehrenfeld, E., Semler, B.L. J. Virol. (2002) [Pubmed]
  11. Crystal structure of the first KH domain of human poly(C)-binding protein-2 in complex with a C-rich strand of human telomeric DNA at 1.7 A. Du, Z., Lee, J.K., Tjhen, R., Li, S., Pan, H., Stroud, R.M., James, T.L. J. Biol. Chem. (2005) [Pubmed]
  12. NMR structures of loop B RNAs from the stem-loop IV domain of the enterovirus internal ribosome entry site: a single C to U substitution drastically changes the shape and flexibility of RNA. Du, Z., Ulyanov, N.B., Yu, J., Andino, R., James, T.L. Biochemistry (2004) [Pubmed]
  13. Requirement of poly(rC) binding protein 2 for translation of poliovirus RNA. Blyn, L.B., Towner, J.S., Semler, B.L., Ehrenfeld, E. J. Virol. (1997) [Pubmed]
  14. Two functional complexes formed by KH domain containing proteins with the 5' noncoding region of poliovirus RNA. Gamarnik, A.V., Andino, R. RNA (1997) [Pubmed]
  15. Interaction of poly(rC)-binding protein 2 with the 5'-terminal stem loop of the hepatitis C-virus genome. Fukushi, S., Okada, M., Kageyama, T., Hoshino, F.B., Nagai, K., Katayama, K. Virus Res. (2001) [Pubmed]
  16. Protein-protein interaction among hnRNPs shuttling between nucleus and cytoplasm. Kim, J.H., Hahm, B., Kim, Y.K., Choi, M., Jang, S.K. J. Mol. Biol. (2000) [Pubmed]
  17. Hepatitis C virus internal ribosome entry site-dependent translation in Saccharomyces cerevisiae is independent of polypyrimidine tract-binding protein, poly(rC)-binding protein 2, and La protein. Rosenfeld, A.B., Racaniello, V.R. J. Virol. (2005) [Pubmed]
  18. Promoter elements and erythroid cell nuclear factors that regulate alpha-globin gene transcription in vitro. Kim, C.G., Swendeman, S.L., Barnhart, K.M., Sheffery, M. Mol. Cell. Biol. (1990) [Pubmed]
  19. Characterization of a family of related cellular transcription factors which can modulate human immunodeficiency virus type 1 transcription in vitro. Yoon, J.B., Li, G., Roeder, R.G. Mol. Cell. Biol. (1994) [Pubmed]
  20. Cellular and molecular effects of a pulse butyrate regimen and new inducers of globin gene expression and hematopoiesis. Ikuta, T., Atweh, G., Boosalis, V., White, G.L., Da Fonseca, S., Boosalis, M., Faller, D.V., Perrine, S.P. Ann. N. Y. Acad. Sci. (1998) [Pubmed]
 
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