Skip Navigation

This Article
Right arrow Full Text Freely available
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 (6)
Right arrowRequest Permissions
Google Scholar
Right arrow Articles by Robson, P.
Right arrow Articles by Keeley, F. W.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Robson, P.
Right arrow Articles by Keeley, F. W.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Molecular Biology and Evolution 17:1739-1752 (2000)
© 2000 Society for Molecular Biology and Evolution

ARTICLE

The Structure and Organization of Lamprin Genes: Multiple-Copy Genes with Alternative Splicing and Convergent Evolution with Insect Structural Proteins

Paul Robson1,*, Glenda M. Wright{dagger}, John H. Youson{ddagger} and Fred W. Keeley

*Division of Cardiovascular Research, Hospital for Sick Children and Department of Biochemistry, University of Toronto, Toronto, Canada;
{dagger}Department of Anatomy and Physiology, Atlantic Veterinary College, University of Prince Edward Island, Charlottetown, Canada; and
{ddagger}Department of Zoology, University of Toronto, Toronto, Canada

Lamprin is a unique structural protein which forms the extracellular matrix of several cartilaginous structures found in the lamprey. Lamprin is noncollagenous in nature but shows sequence similarities to elastins and to insect structural proteins. Here, we characterize the structure and organization of lamprin genes, demonstrating the presence of multiple similar but not identical copies of the lamprin gene in the genome of the lamprey. In at least one species of lamprey, Lampetra richardsoni, the multiple gene copies are arranged in tandem in the genome in a head-to-tail orientation. Lamprin genes from Petromyzon marinus contain either seven or eight exons, with exon 4 being alternatively spliced in all genes, resulting in a total of six different lamprin transcripts. All exon junctions are of class 1,1. An unusual feature of the lamprin gene structure is the distribution of the 3' untranslated region sequence among multiple exons. A TATA box and cap sequence have been identified in upstream sequences in close proximity to the transcription start site, but no CAAT box could be identified. Sequence and gene structure comparisons between lamprins, elastins, and insect structural proteins suggest that the regions of sequence similarity are the result of a process of convergent evolution.


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
 Mol Biol EvolHome page
R. Herranz, J. Mateos, J. A. Mas, E. Garcia-Zaragoza, M. Cervera, and R. Marco
The Coevolution of Insect Muscle TpnT and TpnI Gene Isoforms
Mol. Biol. Evol., November 1, 2005; 22(11): 2231 - 2242.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
B. A. Kozel, H. Wachi, E. C. Davis, and R. P. Mecham
Domains in Tropoelastin That Mediate Elastin Deposition in Vitro and in Vivo
J. Biol. Chem., May 9, 2003; 278(20): 18491 - 18498.
[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.