JBC

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Ohsugi, M.
Right arrow Articles by Yamamoto, T.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Ohsugi, M.
Right arrow Articles by Yamamoto, T.
Social Bookmarking
 Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Volume 272, Number 52, Issue of December 26, 1997 pp. 33092-33099

Molecular Cloning and Characterization of a Novel Cytoplasmic Protein-tyrosine Phosphatase That Is Specifically Expressed in Spermatocytes

(Received for publication, September 19, 1997)

Miho Ohsugi , Satomi Kuramochi , Satoru Matsuda and Tadashi Yamamoto

From the Department of Oncology, Institute of Medical Science, University of Tokyo, 4-6-1 Shirokanedai, Minato-ku Tokyo 108, Japan

We identified a novel gene encoding protein-tyrosine phosphatase using a polymerase chain reaction-based method. Northern blot hybridization of RNAs from various tissues with the polymerase chain reaction-amplified DNA fragment showed that this gene was expressed exclusively in the testis. Complementary DNAs for this gene, termed typ (testis-specific tyrosine phosphatase), were obtained from a mouse testis cDNA library. Nucleotide sequencing of the cDNAs revealed an open reading frame that encoded 426 amino acids. The predicted Typ protein contained a single catalytic domain at the carboxyl-terminal half. No hydrophobic stretch for a possible transmembrane sequence or signal sequence was found, suggesting that Typ is a cytoplasmic protein-tyrosine phosphatase. The amino-terminal half of Typ did not share significant homologies with the other known proteins but contained a region rich in PEST residues. Indirect immunofluorescence studies and in situ hybridization analysis showed that Typ was specifically expressed in testicular germ cells that underwent meiosis. Developmentally, Typ was detected between 2 and 3 weeks after birth, in parallel with the onset of meiosis. Thus, Typ is a new member of the cytoplasmic protein-tyrosine phosphatases that may play an important role(s) in spermatogenesis and/or meiosis.


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
Mol. Cell. Biol.Home page
J. N. Andersen, O. H. Mortensen, G. H. Peters, P. G. Drake, L. F. Iversen, O. H. Olsen, P. G. Jansen, H. S. Andersen, N. K. Tonks, and N. P. H. Moller
Structural and Evolutionary Relationships among Protein Tyrosine Phosphatase Domains
Mol. Cell. Biol., November 1, 2001; 21(21): 7117 - 7136.
[Full Text] [PDF]


Home page
J. Biol. Chem.Home page
K. Aoyama, M. Nagata, K. Oshima, T. Matsuda, and N. Aoki
Molecular Cloning and Characterization of a Novel Dual Specificity Phosphatase, LMW-DSP2, That Lacks the Cdc25 Homology Domain
J. Biol. Chem., July 13, 2001; 276(29): 27575 - 27583.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 1997 by the American Society for Biochemistry and Molecular Biology.