期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1998
卷号：95
期号：18
页码：10517-10522
DOI：10.1073/pnas.95.18.10517
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：Mussel byssal threads contain unusual block copolymer-like proteins that combine collagen with flanking domains that resemble silk-fibroin (preCol-D) or elastin (preCol-P). These are distributed in complementary gradients along the length of the threads and as precursors in the mussel foot. We discuss a 76-kDa precursor, preCol-NG, from a cDNA library of the foot where it has no gradient but rather is distributed evenly along the distal to proximal axis. A pepsin-resistant fragment of preCol-NG has been confirmed in byssal threads. Like preCol-D and -P, this protein has a central collagenous domain, flanking domains, an acidic patch, and histidine-rich termini. The flanking domains of preCol-NG resemble the glycine-rich proteins of plant cell walls with tandem XGlyn repeats where X denotes alanine, leucine, or asparagine but not proline. Similarity with the (glycine-alanine) repeats and poly(alanine) runs of arthropod silks also exists. Based on available evidence, a model of preCol axial assembly is proposed in which preCol-NG functions as a mediator between preCol-D/-P molecules. This is consistent with the observed progression of mechanical properties in byssal threads.
关键词：collagen/glycine-rich cell wall proteins/byssus/ Mytilus /nongradient distribution
