Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1996-1-26
pubmed:databankReference
pubmed:abstractText
We report the characterization of the 5' region of the gene coding for the 2 alpha fibrillar collagen chain of the sea urchin Paracentrotus lividus. This sequence analysis identified the intron/exon organization of the region of the gene coding for the signal peptide, the cysteine-rich domain and the 12 repeats of the four-cysteine module of the unusually long amino-propeptide. This still unknown four-cysteine motif is generally encoded by one exon, which confirms that the distinct amino-propeptide structures of the fibrillar collagens arise from the shuffling of several exon-encoding modules. Moreover, Southern-blot analysis of the sea urchin genome and sequencing of selected genomic clones allowed us to demonstrate that several sea urchin genes could potentially code for the four-cysteine module. Curiously, one of these genes lacks the exons coding for four repeats of this motif while, in another gene, the same exons are submitted to an alternative splicing event.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
234
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
59-65
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Characterization of two genes coding for a similar four-cysteine motif of the amino-terminal propeptide of a sea urchin fibrillar collagen.
pubmed:affiliation
Institut de Biologie et Chimie des Protéines, Centre National de la Recherche Scientifique, Université Claude Bernard, Lyon, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't