An alternative insert of three amino acids is incorporated into collagen XIV in a developmentally regulated fashion
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- 作者：Imhof ; Martin ; Trueb ; Beat
- 关键词：Alternative splicing ; Collagen XIV ; Extracellular matrix ; Fibronectin type III repeat ; FNIII module ; FNIII domain ; fibronectin type III-like domain ; NC4 domain ; domain related to the non-collagenous domain 4 of collagen IX ; RT-PCR ; polymerase chain reacti
- 刊名：FEBS Letters
- 出版年：1998
- 出版时间：November 6, 1998
- 年：1998
- 卷：438
- 期：3
- 页码：325-328
- 全文大小：142 K
文摘
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 β-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.