Purification and domain structure of core hnRNP proteins A1 and A2 and their relationship to single-stranded DNA-binding proteins - PubMed
- ️Wed Jan 01 1986
. 1986 Aug 25;261(24):11266-73.
- PMID: 3733753
Free article
Purification and domain structure of core hnRNP proteins A1 and A2 and their relationship to single-stranded DNA-binding proteins
A Kumar et al. J Biol Chem. 1986.
Free article
Abstract
Protein A1 (Mr approximately 32,000), a major glycine-rich protein of heterogeneous nuclear ribonucleoproteins (hnRNP), was purified to near homogeneity under nondenaturing conditions from HeLa cells. Limited proteolysis of the native protein yields a trypsin-resistant N-terminal nucleic acid-binding domain about 195 amino acids long which has a primary structure nearly identical to that of the 195-amino acid-long single-stranded DNA (ssDNA)-binding protein UP1 (Mr 22,162) from calf thymus (Williams, K.R., Stone, K. L., LoPresti, M.B., Merrill, B. M., and Planck, S.R. (1985) Proc. Natl. Acad. Sci. U.S.A. 82, 5666-5670). 45 of the 61 glycine residues of A1 are present in the trypsin-sensitive C-terminal domain of the protein which contains no sequences homologous to UP1. Protein A2, another major glycine-rich core hnRNP protein from HeLa, has a domain structure analogous to A1 and appears to be related to ssDNA-binding proteins UP1-B from calf liver and HDP-1 from mouse myeloma in a way similar to the A1/UP1 relationship. In contrast to ssDNA-binding proteins, A1 binds preferentially to RNA over ssDNA and exhibits no helix-destabilizing activity.
Similar articles
-
Nadler SG, Merrill BM, Roberts WJ, Keating KM, Lisbin MJ, Barnett SF, Wilson SH, Williams KR. Nadler SG, et al. Biochemistry. 1991 Mar 19;30(11):2968-76. doi: 10.1021/bi00225a034. Biochemistry. 1991. PMID: 1848781
-
Amrute SB, Abdul-Manan Z, Pandey V, Williams KR, Modak MJ. Amrute SB, et al. Biochemistry. 1994 Jul 12;33(27):8282-91. doi: 10.1021/bi00193a015. Biochemistry. 1994. PMID: 7518245
-
Merrill BM, LoPresti MB, Stone KL, Williams KR. Merrill BM, et al. J Biol Chem. 1986 Jan 15;261(2):878-83. J Biol Chem. 1986. PMID: 3941105
-
Recent advances in protein methylation: enzymatic methylation of nucleic acid binding proteins.
Kim S, Park GH, Paik WK. Kim S, et al. Amino Acids. 1998;15(4):291-306. doi: 10.1007/BF01320895. Amino Acids. 1998. PMID: 9891755 Review.
-
Steiner G, Skriner K, Smolen JS. Steiner G, et al. Int Arch Allergy Immunol. 1996 Dec;111(4):314-9. doi: 10.1159/000237386. Int Arch Allergy Immunol. 1996. PMID: 8957102 Review.
Cited by
-
Cloning of the human cDNA for the U1 RNA-associated 70K protein.
Theissen H, Etzerodt M, Reuter R, Schneider C, Lottspeich F, Argos P, Lührmann R, Philipson L. Theissen H, et al. EMBO J. 1986 Dec 1;5(12):3209-17. doi: 10.1002/j.1460-2075.1986.tb04631.x. EMBO J. 1986. PMID: 3028775 Free PMC article.
-
Regulation of BRCA1 transcription by specific single-stranded DNA binding factors.
Thakur S, Nakamura T, Calin G, Russo A, Tamburrino JF, Shimizu M, Baldassarre G, Battista S, Fusco A, Wassell RP, Dubois G, Alder H, Croce CM. Thakur S, et al. Mol Cell Biol. 2003 Jun;23(11):3774-87. doi: 10.1128/MCB.23.11.3774-3787.2003. Mol Cell Biol. 2003. PMID: 12748281 Free PMC article.
-
N(G)-Methylarginines: Biosynthesis, biochemical function and metabolism.
Paik WK, Kim S. Paik WK, et al. Amino Acids. 1993 Oct;4(3):267-86. doi: 10.1007/BF00805828. Amino Acids. 1993. PMID: 24190608
-
Function of conserved domains of hnRNP A1 and other hnRNP A/B proteins.
Mayeda A, Munroe SH, Cáceres JF, Krainer AR. Mayeda A, et al. EMBO J. 1994 Nov 15;13(22):5483-95. doi: 10.1002/j.1460-2075.1994.tb06883.x. EMBO J. 1994. PMID: 7957114 Free PMC article.
-
Burd CG, Swanson MS, Görlach M, Dreyfuss G. Burd CG, et al. Proc Natl Acad Sci U S A. 1989 Dec;86(24):9788-92. doi: 10.1073/pnas.86.24.9788. Proc Natl Acad Sci U S A. 1989. PMID: 2557628 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Molecular Biology Databases