Skip Navigation

This Article
Right arrow FREE Full Text (PDF) Freely available
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in ISI Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (5)
Right arrowRequest Permissions
Google Scholar
Right arrow Articles by Courty, Y.
Right arrow Articles by Rougeon, F.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Courty, Y.
Right arrow Articles by Rougeon, F.
Social Bookmarking
 Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Molecular Biology and Evolution, Vol 13, 758-766, Copyright © 1996 by Society for Molecular Biology and Evolution


ORIGINAL ARTICLE

Episodic evolution and rapid divergence of members of the rat multigene family encoding the salivary prohormone-like protein SMR1

Y Courty, M Singer, I Rosinski-Chupin and F Rougeon
Unite de Genetique et Biochimie du Developpement, Institut Pasteur-URA CNRS, France.

In rodents, the variable coding sequence (VCS) multigene family displays extensive evolutionary divergence in the protein-coding region. While certain VCS genes coding for proline-rich proteins (hPR- PB, mMSG1, rPR-VB1) are conserved in primates and rodents, others seem to be specific to certain genera. This appears to be the case for the Rattus genes forming the A-subclass. This subclass is composed of three genes in R. norvegicus and probably five genes in R. rattus. The first described VCSA gene (Rn. VCSA1) was found to encode a prohormone-like protein named SMR1 (-VA1), expressed mainly in the submandibular glands (SMG) of male rats. To further understand the evolution of this variable multigene family, we have cloned the two additional genes (Rn. VCSA2 and Rn. VCSA3) forming the R. norvegicus A-subclass and three VCSA genes (Rr. VCSA1a, b and Rr. VCSA2) of R. rattus. The putative SMR1 proteins encoded by all these genes display the same prohormone- like structure as Rn. SMR1-VA1. However, we observe a polymorphism in some internal cleavage sites which suggests that multiple processing of the SMR1 proteins could result in the liberation of peptides differing in structure and length. The phylogenetic analysis of the sequences reveals that the duplication events giving rise to the VCSA1, -A2, and - A3 progenitors were anterior to the R. norvegicus and R. rattus split, and that a VCSA1 duplication event likely occurred specifically in R. rattus. A striking observation is that the coding sequences of the VCSA genes have rapidly diverged from their ancestors. Along all branches of the phylogeny, the nonsynonymous divergence rate is identical or superior to the synonymous divergence rate. We suggest that frequent changes in functional requirements are mainly responsible for the episodic evolution and the rapid divergence of the VCSA genes.
Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
EndocrinologyHome page
I. Rosinski-Chupin, J.-F. Huaulme, C. Rougeot, and F. Rougeon
The Transcriptional Response to Androgens of the Rat VCSA1 Gene Is Amplified by Both Binary and Graded Mechanisms
Endocrinology, October 1, 2001; 142(10): 4550 - 4559.
[Abstract] [Full Text] [PDF]


Home page
Mol Biol EvolHome page
T. F. Duda Jr and S. R. Palumbi
Evolutionary Diversification of Multigene Families: Allelic Selection of Toxins in Predatory Cone Snails
Mol. Biol. Evol., September 1, 2000; 17(9): 1286 - 1293.
[Abstract] [Full Text] [PDF]


Home page
J. Histochem. Cytochem.Home page
M. Señorale–Pose, A. Jacqueson, F. Rougeon, and I. Rosinski–Chupin
Acinar Cells Are Target Cells for Androgens in Mouse Submandibular Glands
J. Histochem. Cytochem., May 1, 1998; 46(5): 669 - 678.
[Abstract] [Full Text]


Home page
Am. J. Physiol. Regul. Integr. Comp. Physiol.Home page
C. Rougeot, R. Vienet, A. Cardona, L. Le Doledec, J. M. Grognet, and F. Rougeon
Targets for SMR1-pentapeptide suggest a link between the circulating peptide and mineral transport
Am J Physiol Regulatory Integrative Comp Physiol, October 1, 1997; 273(4): R1309 - R1320.
[Abstract] [Full Text] [PDF]



Disclaimer:
Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.