Jump to ContentJump to Main Navigation
Show Summary Details
More options …

Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

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

12 Issues per year


IMPACT FACTOR 2017: 3.022

CiteScore 2017: 2.81

SCImago Journal Rank (SJR) 2017: 1.562
Source Normalized Impact per Paper (SNIP) 2017: 0.705

Online
ISSN
1437-4315
See all formats and pricing
More options …
Volume 388, Issue 9

Issues

Josephin domain-containing proteins from a variety of species are active de-ubiquitination enzymes

Nikolay Tzvetkov
  • 1Department of Cellular Biochemistry, Max-Planck Institute of Biochemistry, Am Klopferspitz 18, D-82152 Martinsried, Germany and Present addresses: Institute of Biophysical Chemistry, Hannover Medical School, Carl-Neuberg-Strasse 1, D-30623 Hannover, Germany
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Peter Breuer
  • 2Department of Cellular Biochemistry, Max-Planck Institute of Biochemistry, Am Klopferspitz 18, D-82152 Martinsried, Germany and Department of Neurology, University of Bonn, Sigmund-Freud-Strasse 25, D-53105 Bonn, Germany.
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
Published Online: 2007-08-14 | DOI: https://doi.org/10.1515/BC.2007.107

Abstract

The neurodegenerative disease spinocerebellar ataxia type 3 (SCA3) is caused by the presence of an extended polyglutamine stretch (polyQ) in the unstructured C-terminus of the human ataxin-3 (AT3) protein. The structured N-terminal Josephin domain (JD) of AT3 is conserved within a novel family of potential ubiquitin proteases, the JD-containing proteins, which are sub-divided into two groups termed ataxins and Josephins. These AT3 orthologs are encoded by the genomes of organisms ranging from Plasmodium falciparum to humans, with most species possessing more than one homolog. While Josephins consist of JDs alone, ataxins contain additional functional domains that may influence their enzyme activity. Here, we show that the enzyme activity of human AT3 (hAT3) is not affected by the length of polyQ in its C-terminus, even when it is in the range associated with SCA3. We also show that JDs of all human proteins with homology to AT3 and its homologs from various species possess de-ubiquitination activity. These results establish JD-containing proteins as a novel family of active de-ubiquitination enzymes with wide phylogenic distribution.

Keywords: ataxin-3; de-ubiquitination; neurodegenerative diseases; polyglutamine proteins; protein misfolding

About the article

Corresponding author


Received: 2007-05-11

Accepted: 2007-05-24

Published Online: 2007-08-14

Published in Print: 2007-09-01


Citation Information: Biological Chemistry, Volume 388, Issue 9, Pages 973–978, ISSN (Online) 14374315, ISSN (Print) 14316730, DOI: https://doi.org/10.1515/BC.2007.107.

Export Citation

Citing Articles

Here you can find all Crossref-listed publications in which this article is cited. If you would like to receive automatic email messages as soon as this article is cited in other publications, simply activate the “Citation Alert” on the top of this page.

[1]
April Darling and Vladimir Uversky
Molecules, 2017, Volume 22, Number 12, Page 2027
[2]
Lodewijk J.A. Toonen, Frank Rigo, Haico van Attikum, and Willeke M.C. van Roon-Mom
Molecular Therapy - Nucleic Acids, 2017, Volume 8, Page 232
[3]
Stephen D. Weeks, Kimberly C. Grasty, Lisa Hernandez-Cuebas, and Patrick J. Loll
Journal of Biological Chemistry, 2011, Volume 286, Number 6, Page 4555
[4]
Takahiro Seki, Lijie Gong, Aislinn J. Williams, Norio Sakai, Sokol V. Todi, and Henry L. Paulson
Journal of Biological Chemistry, 2013, Volume 288, Number 24, Page 17145
[5]
Maria do Carmo Costa, Fernanda Bajanca, Ana-João Rodrigues, Ricardo J. Tomé, Garry Corthals, Sandra Macedo-Ribeiro, Henry L. Paulson, Elsa Logarinho, Patrícia Maciel, and Christoph Winkler
PLoS ONE, 2010, Volume 5, Number 7, Page e11728
[6]
Mahmood Rasool, Arif Malik, Muhammad Imran Naseer, Abdul Manan, Shakeel Ahmed Ansari, Irshad Begum, Mahmood Husain Qazi, Peter Natesan Pushparaj, Adel M Abuzenadah, Mohammed Hussein Al-Qahtani, Mohammad Amjad Kamal, and Siew Hua Gan
BMC Medical Genomics, 2015, Volume 8, Number S1
[7]
Roberta Verciano Pereira, Matheus de Souza Gomes, Marcela Pereira Costa, Liana Konovaloff Jannotti Passos, William de Castro Borges, and Renata Guerra-Sá
Parasitology Research, 2015, Volume 114, Number 8, Page 2835
[8]
Ziad M. Eletr and Keith D. Wilkinson
Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, 2014, Volume 1843, Number 1, Page 114
[9]
Benedikt M Kessler
Current Opinion in Chemical Biology, 2013, Volume 17, Number 1, Page 59
[10]
Y. A. Yao, J. Wang, X. Ma, S. Lutts, C. Sun, J. Ma, Y. Yang, V. Achal, and G. Xu
Journal of Experimental Botany, 2012, Volume 63, Number 14, Page 5155
[11]
Carlos A. Matos, Sandra de Macedo-Ribeiro, and Ana Luísa Carvalho
Progress in Neurobiology, 2011, Volume 95, Number 1, Page 26
[12]
Conceição Bettencourt and Manuela Lima
Orphanet Journal of Rare Diseases, 2011, Volume 6, Number 1, Page 35
[13]
Thomas M. Durcan, Maria Kontogiannea, Thorhildur Thorarinsdottir, Lara Fallon, Aislinn J. Williams, Ana Djarmati, Tadeu Fantaneanu, Henry L. Paulson, and Edward A. Fon
Human Molecular Genetics, 2011, Volume 20, Number 1, Page 141
[14]
Xiao-Hui He, Fang Lin, and Zheng-Hong Qin
Neuroscience Bulletin, 2010, Volume 26, Number 3, Page 247
[15]
Conceição Bettencourt, Cristina Santos, Rafael Montiel, Maria do Carmo Costa, Pablo Cruz-Morales, Liliana Ribeiro Santos, Nelson Simões, Teresa Kay, João Vasconcelos, Patrícia Maciel, and Manuela Lima
neurogenetics, 2010, Volume 11, Number 2, Page 193

Comments (0)

Please log in or register to comment.
Log in