A large DNA-binding nuclear protein with RNA recognition motif and serine/arginine-rich domain

Hidetoshi Inagaki, Yuichi Matsushima, Kazuyasu Nakamura, Mikiko Ohshima, Tatsuhiko Kadowaki, Yasuo Kitagawa

Research output: Contribution to journalArticle

30 Citations (Scopus)

Abstract

cDNA species encoding a large DNA-binding protein (NP220) of 1978 amino acids was isolated from human cDNA libraries. Human NP220 binds to double- stranded DNA fragments by recognizing clusters of cytidines. Immunofluorescent microscopy with antiserum directed against NP220 revealed a punctate or 'speckled' pattern and coiled body-like structures in the nucleoplasm of various human cell lines. These structures diffused in the cytoplasm during mitosis. Western blot analysis showed that NP220 is enriched in the lithium 3,5-diiodosalicylate-insoluble fraction of nuclei. The domain essential for DNA binding is localized in C-terminal half of NP220. Human NP220 shares three types of domains (MH1, MH2, and MH3) with the acidic nuclear protein, matrin 3 (Belgrader, P., Dey, R., and Berezney, R. (1991) J. Biol. Chem. 266, 9893-9899). MH1 is a 48-amino acid sequence near the N terminus of both human NP220 and rat matrin 3. MH2 is a 75-amino acid sequence homologous to the RNA recognition motifs of heterogeneous nuclear RNP I and L. It is repeated three times in NP220 and twice in matrin 3. MH3 is a 60-amino acid sequence at the C terminus of both NP220 and matrin 3. NP220 has an arginine/serine-rich domain commonly found in pre-mRNA splicing factors. Close to the domain essential for DNA binding, there are nine repeats of the sequence LVTVDEVIEEEDL. Thus, NP220 is a novel type of nucleoplasmic protein with multiple domains.

Original languageEnglish
Pages (from-to)12525-12531
Number of pages7
JournalJournal of Biological Chemistry
Volume271
Issue number21
DOIs
Publication statusPublished - May 28 1996

Fingerprint

DNA-Binding Proteins
Nuclear Proteins
Serine
Arginine
RNA
Amino Acids
DNA
Amino Acid Sequence
Coiled Bodies
Cytidine
RNA Precursors
Amino Acid Sequence Homology
Gene Library
Lithium
Immune Sera
Microscopic examination
Mitosis
Complementary DNA
Cells
Microscopy

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

A large DNA-binding nuclear protein with RNA recognition motif and serine/arginine-rich domain. / Inagaki, Hidetoshi; Matsushima, Yuichi; Nakamura, Kazuyasu; Ohshima, Mikiko; Kadowaki, Tatsuhiko; Kitagawa, Yasuo.

In: Journal of Biological Chemistry, Vol. 271, No. 21, 28.05.1996, p. 12525-12531.

Research output: Contribution to journalArticle

Inagaki, Hidetoshi ; Matsushima, Yuichi ; Nakamura, Kazuyasu ; Ohshima, Mikiko ; Kadowaki, Tatsuhiko ; Kitagawa, Yasuo. / A large DNA-binding nuclear protein with RNA recognition motif and serine/arginine-rich domain. In: Journal of Biological Chemistry. 1996 ; Vol. 271, No. 21. pp. 12525-12531.
@article{13fb7ab8e8f6412fa5767054a567986a,
title = "A large DNA-binding nuclear protein with RNA recognition motif and serine/arginine-rich domain",
abstract = "cDNA species encoding a large DNA-binding protein (NP220) of 1978 amino acids was isolated from human cDNA libraries. Human NP220 binds to double- stranded DNA fragments by recognizing clusters of cytidines. Immunofluorescent microscopy with antiserum directed against NP220 revealed a punctate or 'speckled' pattern and coiled body-like structures in the nucleoplasm of various human cell lines. These structures diffused in the cytoplasm during mitosis. Western blot analysis showed that NP220 is enriched in the lithium 3,5-diiodosalicylate-insoluble fraction of nuclei. The domain essential for DNA binding is localized in C-terminal half of NP220. Human NP220 shares three types of domains (MH1, MH2, and MH3) with the acidic nuclear protein, matrin 3 (Belgrader, P., Dey, R., and Berezney, R. (1991) J. Biol. Chem. 266, 9893-9899). MH1 is a 48-amino acid sequence near the N terminus of both human NP220 and rat matrin 3. MH2 is a 75-amino acid sequence homologous to the RNA recognition motifs of heterogeneous nuclear RNP I and L. It is repeated three times in NP220 and twice in matrin 3. MH3 is a 60-amino acid sequence at the C terminus of both NP220 and matrin 3. NP220 has an arginine/serine-rich domain commonly found in pre-mRNA splicing factors. Close to the domain essential for DNA binding, there are nine repeats of the sequence LVTVDEVIEEEDL. Thus, NP220 is a novel type of nucleoplasmic protein with multiple domains.",
author = "Hidetoshi Inagaki and Yuichi Matsushima and Kazuyasu Nakamura and Mikiko Ohshima and Tatsuhiko Kadowaki and Yasuo Kitagawa",
year = "1996",
month = "5",
day = "28",
doi = "10.1074/jbc.271.21.12525",
language = "English",
volume = "271",
pages = "12525--12531",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "21",

}

TY - JOUR

T1 - A large DNA-binding nuclear protein with RNA recognition motif and serine/arginine-rich domain

AU - Inagaki, Hidetoshi

AU - Matsushima, Yuichi

AU - Nakamura, Kazuyasu

AU - Ohshima, Mikiko

AU - Kadowaki, Tatsuhiko

AU - Kitagawa, Yasuo

PY - 1996/5/28

Y1 - 1996/5/28

N2 - cDNA species encoding a large DNA-binding protein (NP220) of 1978 amino acids was isolated from human cDNA libraries. Human NP220 binds to double- stranded DNA fragments by recognizing clusters of cytidines. Immunofluorescent microscopy with antiserum directed against NP220 revealed a punctate or 'speckled' pattern and coiled body-like structures in the nucleoplasm of various human cell lines. These structures diffused in the cytoplasm during mitosis. Western blot analysis showed that NP220 is enriched in the lithium 3,5-diiodosalicylate-insoluble fraction of nuclei. The domain essential for DNA binding is localized in C-terminal half of NP220. Human NP220 shares three types of domains (MH1, MH2, and MH3) with the acidic nuclear protein, matrin 3 (Belgrader, P., Dey, R., and Berezney, R. (1991) J. Biol. Chem. 266, 9893-9899). MH1 is a 48-amino acid sequence near the N terminus of both human NP220 and rat matrin 3. MH2 is a 75-amino acid sequence homologous to the RNA recognition motifs of heterogeneous nuclear RNP I and L. It is repeated three times in NP220 and twice in matrin 3. MH3 is a 60-amino acid sequence at the C terminus of both NP220 and matrin 3. NP220 has an arginine/serine-rich domain commonly found in pre-mRNA splicing factors. Close to the domain essential for DNA binding, there are nine repeats of the sequence LVTVDEVIEEEDL. Thus, NP220 is a novel type of nucleoplasmic protein with multiple domains.

AB - cDNA species encoding a large DNA-binding protein (NP220) of 1978 amino acids was isolated from human cDNA libraries. Human NP220 binds to double- stranded DNA fragments by recognizing clusters of cytidines. Immunofluorescent microscopy with antiserum directed against NP220 revealed a punctate or 'speckled' pattern and coiled body-like structures in the nucleoplasm of various human cell lines. These structures diffused in the cytoplasm during mitosis. Western blot analysis showed that NP220 is enriched in the lithium 3,5-diiodosalicylate-insoluble fraction of nuclei. The domain essential for DNA binding is localized in C-terminal half of NP220. Human NP220 shares three types of domains (MH1, MH2, and MH3) with the acidic nuclear protein, matrin 3 (Belgrader, P., Dey, R., and Berezney, R. (1991) J. Biol. Chem. 266, 9893-9899). MH1 is a 48-amino acid sequence near the N terminus of both human NP220 and rat matrin 3. MH2 is a 75-amino acid sequence homologous to the RNA recognition motifs of heterogeneous nuclear RNP I and L. It is repeated three times in NP220 and twice in matrin 3. MH3 is a 60-amino acid sequence at the C terminus of both NP220 and matrin 3. NP220 has an arginine/serine-rich domain commonly found in pre-mRNA splicing factors. Close to the domain essential for DNA binding, there are nine repeats of the sequence LVTVDEVIEEEDL. Thus, NP220 is a novel type of nucleoplasmic protein with multiple domains.

UR - http://www.scopus.com/inward/record.url?scp=17544370939&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=17544370939&partnerID=8YFLogxK

U2 - 10.1074/jbc.271.21.12525

DO - 10.1074/jbc.271.21.12525

M3 - Article

VL - 271

SP - 12525

EP - 12531

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 21

ER -