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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred


IMPACT FACTOR 2018: 3.014
5-year IMPACT FACTOR: 3.162

CiteScore 2018: 3.09

SCImago Journal Rank (SJR) 2018: 1.482
Source Normalized Impact per Paper (SNIP) 2018: 0.820

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1437-4315
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Volume 390, Issue 1

Issues

The ADP-ribosylating thermozyme from Sulfolobus solfataricus is a DING protein

Antimo Di Maro
  • 1Department of Life Sciences, Faculty of Sciences M.F.N., Second University of Naples, Via Vivadi 45, I-81100 Caserta, Italy
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/ Anna De Maio
  • 2Department of Structural and Functional Biology, Faculty of Sciences M.F.N., University of Naples ‘Federico II’, Via Cinthia, I-80126 Naples, Italy and National Institute of Biostructures and Biosystems (INBB), Viale medaglie d'oro 305, I-00136 Rome, Italy
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/ Sabrina Castellano
  • 3Department of Structural and Functional Biology, Faculty of Sciences M.F.N., University of Naples ‘Federico II’, Via Cinthia, I-80126 Naples, Italy
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/ Augusto Parente
  • 4Department of Life Sciences, Faculty of Sciences M.F.N., Second University of Naples, Via Vivadi 45, I-81100 Caserta, Italy
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/ Benedetta Farina
  • 5Department of Structural and Functional Biology, Faculty of Sciences M.F.N., University of Naples ‘Federico II’, Via Cinthia, I-80126 Naples, Italy and National Institure of Biostructures and Biosystems (INBB), Viale medaglie d'oro 305, I-00136 Rome, Italy
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/ Maria Rosaria Faraone-Mennella
  • 6Department of Structural and Functional Biology, Faculty of Sciences M.F.N., University of Naples ‘Federico II’, Via Cinthia, I-80126 Naples, Italy and National Institute of Biostructures and Biosystems (INBB), Viale medaglie d'oro 305, I-00136 Rome, Italy
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Published Online: 2008-11-13 | DOI: https://doi.org/10.1515/BC.2009.006

Abstract

The partial amino acid sequence of the sulfolobal thermoprotein biochemically characterized as poly(ADP-ribose)polymerase-like enzyme overlaps those of DING proteins. This group of proteins, widely occurring in animals, plants and eubacteria, shows a characteristic and highly conserved N-terminus, DINGGGATL. The sequence of the N-terminal region and of the analyzed tryptic peptides of the sulfolobal thermozyme shows a high similarity with most of the DING proteins from databases. This is the first example of a DING protein from a sulfolobal source.

Keywords: archaeon; Edman degradation; DING protein; poly(ADP-ribose) polymerase; Sulfolobus solfataricus; thermoprotein

About the article

Corresponding author


Received: 2008-07-15

Accepted: 2008-09-29

Published Online: 2008-11-13

Published in Print: 2009-01-01


Citation Information: Biological Chemistry, Volume 390, Issue 1, Pages 27–30, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.2009.006.

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