Sequence basis of Barnacle Cement Nanostructure is Defined by Proteins with Silk Homology.

Published

Journal Article

Barnacles adhere by producing a mixture of cement proteins (CPs) that organize into a permanently bonded layer displayed as nanoscale fibers. These cement proteins share no homology with any other marine adhesives, and a common sequence-basis that defines how nanostructures function as adhesives remains undiscovered. Here we demonstrate that a significant unidentified portion of acorn barnacle cement is comprised of low complexity proteins; they are organized into repetitive sequence blocks and found to maintain homology to silk motifs. Proteomic analysis of aggregate bands from PAGE gels reveal an abundance of Gly/Ala/Ser/Thr repeats exemplified by a prominent, previously unidentified, 43 kDa protein in the solubilized adhesive. Low complexity regions found throughout the cement proteome, as well as multiple lysyl oxidases and peroxidases, establish homology with silk-associated materials such as fibroin, silk gum sericin, and pyriform spidroins from spider silk. Distinct primary structures defined by homologous domains shed light on how barnacles use low complexity in nanofibers to enable adhesion, and serves as a starting point for unraveling the molecular architecture of a robust and unique class of adhesive nanostructures.

Full Text

Duke Authors

Cited Authors

  • So, CR; Fears, KP; Leary, DH; Scancella, JM; Wang, Z; Liu, JL; Orihuela, B; Rittschof, D; Spillmann, CM; Wahl, KJ

Published Date

  • November 8, 2016

Published In

Volume / Issue

  • 6 /

Start / End Page

  • 36219 -

PubMed ID

  • 27824121

Pubmed Central ID

  • 27824121

Electronic International Standard Serial Number (EISSN)

  • 2045-2322

International Standard Serial Number (ISSN)

  • 2045-2322

Digital Object Identifier (DOI)

  • 10.1038/srep36219

Language

  • eng