An alternative insert of three amino acids is incorporated into collagen XIV in a developmentally regulated fashion.
We have identified a novel splice variant of chicken collagen XIV which contains an insert of three amino acids (Val-Arg-Thr) in the sixth fibronectin type III-like (FNIII) domain. The codons for these amino acids are inserted into the mRNA by skipping of a splice donor site and usage of another donor site 9 bp further downstream in the collagen XIV gene. The percentage of the new splice variant in the total collagen XIV mRNA varies between 22 and 46% in different embryonic tissues. After hatching, however, this percentage increases dramatically and reaches 86% in adult skeletal muscle and 58% in adult gizzard, indicating developmental regulation of this splicing event. Computer modeling suggests that the three extra amino acids cause an increase in the size of a flexible loop connecting two beta-strands in the sixth FNIII domain. This increase might affect the exact arrangement of the FNIII domain in the collagen XIV molecule, thereby modulating its interactions with other matrix molecules.
Imhof
M
M
M.E. Müller-Institute for Biomechanics, University of Bern, Switzerland.
Trueb
B
B
D017398:Alternative Splicing; D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002642:Chick Embryo; D002645:Chickens; D003094:Collagen / Q000096:biosynthesis / Q000737:chemistry* / Q000235:genetics*; D003198:Computer Simulation; D004251:DNA Transposable Elements; D005347:Fibroblasts; D018507:Gene Expression Regulation, Developmental; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009928:Organ Specificity; D017433:Protein Structure, Secondary; D014158:Transcription, Genetic
D004251:DNA Transposable Elements; D003094:Collagen