Mammalian single-stranded DNA binding protein UP I is derived from the hnRNP core protein A1.

S. Riva, C. Morandi, Pantelis Tsoulfas, M. Pandolfo, G. Biamonti, B. Merrill, K. R. Williams, G. Multhaup, K. Beyreuther, H. Werr

Research output: Contribution to journalArticle

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Abstract

Antibodies induced against mammalian single-stranded DNA binding protein (ssDBP) UP I were shown to be cross-reactive with most of the basic hnRNP core proteins, the main constituents of 40S hnRNP particles. This suggested a structural relationship between both groups of proteins. Using the anti-ssDBP antibodies, a cDNA clone (pRP10) was isolated from a human liver cDNA library in plasmid expression vector pEX1. By DNA sequencing this clone was shown to encode in its 949 bp insert the last 72 carboxy terminal amino acids of the ssDBP UP I. Thereafter, an open reading frame continued for another 124 amino acids followed by a UAA (ochre) stop codon. Direct amino acid sequencing of a V8 protease peptide from hnRNP core protein A1 showed that this peptide contained at its amino terminus the last 11 amino acids of UP I followed by 19 amino acids which are encoded by the open reading frame of cDNA clone pRP10 immediately following the UP I sequence. This proves that ssDBP UP I arises by proteolysis from hnRNP core protein A1. This finding must lead to a re-evaluation of the possible physiological role of UP I and related ssDBPs. The formerly assumed function in DNA replication, although not completely ruled out, should be reconsidered in the light of a possible alternative or complementary function in hnRNA processing where UP I could either be a simple degradation product of core protein A1 (as a consequence of controlling the levels of active A1) or may continue to function as an RNA binding protein which has lost the ability to interact with the other core proteins.(ABSTRACT TRUNCATED AT 250 WORDS)

Original languageEnglish (US)
Pages (from-to)2267-2273
Number of pages7
JournalThe EMBO journal
Volume5
Issue number9
StatePublished - Sep 1 1986
Externally publishedYes

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Heterogeneous-Nuclear Ribonucleoproteins
DNA-Binding Proteins
Amino Acids
Clone Cells
Terminator Codon
Open Reading Frames
Proteins
Complementary DNA
Peptides
RNA-Binding Proteins
Antibodies
Protein Sequence Analysis
DNA Replication
Gene Library
DNA Sequence Analysis
Proteolysis
Plasmids
DNA
Liver
hnRNP A1

ASJC Scopus subject areas

  • Neuroscience(all)
  • Molecular Biology
  • Biochemistry, Genetics and Molecular Biology(all)
  • Immunology and Microbiology(all)

Cite this

Riva, S., Morandi, C., Tsoulfas, P., Pandolfo, M., Biamonti, G., Merrill, B., ... Werr, H. (1986). Mammalian single-stranded DNA binding protein UP I is derived from the hnRNP core protein A1. The EMBO journal, 5(9), 2267-2273.

Mammalian single-stranded DNA binding protein UP I is derived from the hnRNP core protein A1. / Riva, S.; Morandi, C.; Tsoulfas, Pantelis; Pandolfo, M.; Biamonti, G.; Merrill, B.; Williams, K. R.; Multhaup, G.; Beyreuther, K.; Werr, H.

In: The EMBO journal, Vol. 5, No. 9, 01.09.1986, p. 2267-2273.

Research output: Contribution to journalArticle

Riva, S, Morandi, C, Tsoulfas, P, Pandolfo, M, Biamonti, G, Merrill, B, Williams, KR, Multhaup, G, Beyreuther, K & Werr, H 1986, 'Mammalian single-stranded DNA binding protein UP I is derived from the hnRNP core protein A1.', The EMBO journal, vol. 5, no. 9, pp. 2267-2273.
Riva S, Morandi C, Tsoulfas P, Pandolfo M, Biamonti G, Merrill B et al. Mammalian single-stranded DNA binding protein UP I is derived from the hnRNP core protein A1. The EMBO journal. 1986 Sep 1;5(9):2267-2273.
Riva, S. ; Morandi, C. ; Tsoulfas, Pantelis ; Pandolfo, M. ; Biamonti, G. ; Merrill, B. ; Williams, K. R. ; Multhaup, G. ; Beyreuther, K. ; Werr, H. / Mammalian single-stranded DNA binding protein UP I is derived from the hnRNP core protein A1. In: The EMBO journal. 1986 ; Vol. 5, No. 9. pp. 2267-2273.
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abstract = "Antibodies induced against mammalian single-stranded DNA binding protein (ssDBP) UP I were shown to be cross-reactive with most of the basic hnRNP core proteins, the main constituents of 40S hnRNP particles. This suggested a structural relationship between both groups of proteins. Using the anti-ssDBP antibodies, a cDNA clone (pRP10) was isolated from a human liver cDNA library in plasmid expression vector pEX1. By DNA sequencing this clone was shown to encode in its 949 bp insert the last 72 carboxy terminal amino acids of the ssDBP UP I. Thereafter, an open reading frame continued for another 124 amino acids followed by a UAA (ochre) stop codon. Direct amino acid sequencing of a V8 protease peptide from hnRNP core protein A1 showed that this peptide contained at its amino terminus the last 11 amino acids of UP I followed by 19 amino acids which are encoded by the open reading frame of cDNA clone pRP10 immediately following the UP I sequence. This proves that ssDBP UP I arises by proteolysis from hnRNP core protein A1. This finding must lead to a re-evaluation of the possible physiological role of UP I and related ssDBPs. The formerly assumed function in DNA replication, although not completely ruled out, should be reconsidered in the light of a possible alternative or complementary function in hnRNA processing where UP I could either be a simple degradation product of core protein A1 (as a consequence of controlling the levels of active A1) or may continue to function as an RNA binding protein which has lost the ability to interact with the other core proteins.(ABSTRACT TRUNCATED AT 250 WORDS)",
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AU - Morandi, C.

AU - Tsoulfas, Pantelis

AU - Pandolfo, M.

AU - Biamonti, G.

AU - Merrill, B.

AU - Williams, K. R.

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