Specificity in the coacervation of tropoelastin: solvent exposed lysines

详细信息    查看全文

• 作者：Wise ; Steven G. ; Mithieux ; Suzanne M. ; Raftery ; Mark J. ; Weiss ; Anthony S.
• 关键词：Elastin ; Cross-linking ; BS3 ; Tropoelastin ; Coacervation ; Assembly
• 刊名：Journal of Structural Biology
• 出版年：2005
• 出版时间：March, 2005
• 年：2005
• 卷：149
• 期：3
• 页码：273-281
• 全文大小：544 K

文摘

Tropoelastin protein monomers associate by coacervation and are cross-linked in vivo to form elastin macro-assemblies. We provide evidence for specific protein domain contact points between tropoelastin monomers during association by coacervation. The homobifunctional cross-linker bis(sulfosuccinimidyl) suberate served as a rapid reporter of adjacent lysines and preferentially exposed domains. Intact cross-linked peptide pairs were identified after protease digestion and high-resolution electrospray mass spectrometry followed by MS/MS sequencing. Mapping of the assigned sequences indicated that the region in the monomer spanning domains 19aaa25 was readily accessible to solvent and enriched in cross-linking. Domains 12 and 36 were also prevalent, where these two regions were not previously thought to play a major role in the formation of mature elastin. A specificity for particular lysines allowed for the construction of a model for the first close contacts between domains and the first detailed study of the cross-linking of tropoelastin.