HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

J. Biol. Chem., Vol. 277, Issue 5, 3632-3639, February 1, 2002

This Article Full Text Full Text (PDF) All Versions of this Article: 277/5/3632    most recent M107578200v1 Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Lin, H.-J. Articles by Chen, Y.-H. Search for Related Content PubMed PubMed Citation Articles by Lin, H.-J. Articles by Chen, Y.-H. Social Bookmarking                      What's this?

Localization of the Transglutaminase Cross-linking Site in SVS III, a Novel Glycoprotein Secreted from Mouse Seminal Vesicle^*

Han-Jia Lin^§, Ching-Wei Luo^¶, and Yee-Hsiung Chen^¶

From the  Institute of Biochemical Sciences, College of Science, National Taiwan University and ^¶ Institute of Biological Chemistry, Academia Sinica, Taipei 106, Taiwan

The nucleotide sequence of MpSv-1, a novel androgen-regulated gene exclusively expressed in mouse seminal vesicle, was analyzed to establish a 5'-flanking region of 2123 bp, three exons of 95, 765, and 330 bp, and two introns of 222 and 811 bp. The transcription unit is organized with the first exon encoding a signal peptide, and the second a secreted protein, whereas the third encompasses a 3'-non-translated nucleotide that shares common features of rapid evolving substrates of transglutaminase gene family. The protein sequence deduced from this gene contains 265 amino acid residues in which the central part, residues 116-145, is a region composed of five short tandem repeats, consisting of four amino acid residues, QXK(S/T), where X is an aliphatic amino acid residue. Among the mouse seminal vesicle secretory proteins that could be resolved by SDS-PAGE into seven major components, SVS I-VII, the antiserum against residues 77-109 of the MpSv-1-translated protein only reacted with SVS III. Matrix-assisted laser desorption/ionization-time of flight mass spectral analysis from a trypsin digest of SVS III supported this protein as derived from MpSv-1. SVS III was immunolocalized to the epithelium of both the primary and secondary folds of the seminal vesicle and the copulatory plug. All of mouse SVS I-III were proven to be substrates of transglutaminase and could be cross-linked readily after the enzyme reaction. The transglutaminase cross-linking site of SVS III was identified to be the tandem repeats of QXK(S/T) in the central part of this protein molecule.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBank^TM/EBI Data Bank with accession number(s) AF323459.

CiteULike

Complore

Connotea

Del.icio.us

Digg

Reddit

Technorati

This article has been cited by other articles:

				R. C. Karn, N. L. Clark, E. D. Nguyen, and W. J. Swanson Adaptive Evolution in Rodent Seminal Vesicle Secretion Proteins Mol. Biol. Evol., November 1, 2008; 25(11): 2301 - 2310. [Abstract] [Full Text] [PDF]