Molecular mapping of statherin- and histatin-binding domains in human salivary mucin MG1 (MUC5B) by the yeast two-hybrid system.

Molecular mapping of statherin- and histatin-binding domains in human salivary mucin MG1 (MUC5B) by the yeast two-hybrid system. Research Abstract Details 

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Molecular mapping of statherin- and histatin-binding domains in human salivary mucin MG1 (MUC5B) by the yeast two-hybrid system. Abstract Text:

I Iontcheva,F G Oppenheim,G D Offner,R F Troxler,

MGI is a high-molecular-weight mucin secreted by mucous acinar cells in human submandibular and sublingual glands. We have recently shown that the tracheobronchial mucin MUC5B is a major component of MG1. MUC5B is organized into cysteine-rich N- and C-terminal regions that flank a central tandem-repeat region containing cysteine-rich subdomains and imperfect 29-residue tandem repeats. In earlier work, we have shown that this mucin selectively forms heterotypic complexes with amylase, proline-rich proteins, statherin, and histatins in salivary secretions, and the aim of this study was to identify specific binding domains within MUC5B using the yeast two-hybrid system. Interactions of cysteine-rich domains in the tandem-repeat region (Cys1-Cys4) and C-terminal region (Cys8a, Cys8b, Cys8c) of MUC5B with statherin and histatins were investigated. These studies indicated that histatin 1 selectively bound to Cysl and Cys2, whereas statherin and histatin 1, 3, and 5 selectively bound to Cys8a. Analysis of the primary sequences of the identified binding domains suggests that these domains most probably can fold into globular-like structures in the native mucin. A ProDom blast search revealed that sequences in Cys1, Cys2, and Cys8a exhibit similarity to domains in evolutionarily diverse extracellular proteins known to participate in a wide variety of protein-protein interactions.

Molecular mapping of statherin- and histatin-binding domains in human salivary mucin MG1 (MUC5B) by the yeast two-hybrid system. Publishing Authors By Initials

I Iontcheva,FG Oppenheim,GD Offner,RF Troxler,

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Molecular mapping of statherin- and histatin-binding domains in human salivary mucin MG1 (MUC5B) by the yeast two-hybrid system. Journal Published:

PUBLICATION TYPE: Research Support, U.S. Gov't,

Journal: Journal of dental research

VOLUME: 79

Page Numbers: 732-9

Journal Abbreviation: J. Dent. Res.

ISSN: 0022-0345

DAY: 29

MONTH: Feb

YEAR: 2000

Molecular mapping of statherin- and histatin-binding domains in human salivary mucin MG1 (MUC5B) by the yeast two-hybrid system. Information

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LANGUAGE: eng

NlmUniqueID: 354343

Molecular mapping of statherin- and histatin-binding domains in human salivary mucin MG1 (MUC5B) by the yeast two-hybrid system. Keywords Mesh Terms:

KEYWORDS: Yeasts

MESH TERMS: genetics

Chemical & Substance for Abstract: Molecular mapping of statherin- and histatin-binding domains in human salivary mucin MG1 (MUC5B) by the yeast two-hybrid system. Information

Substance Name: Amylases

Registry Number: EC 3.2.1.-

Grant and Affiliation Information for Molecular mapping of statherin- and histatin-binding domains in human salivary mucin MG1 (MUC5B) by the yeast two-hybrid system.

AFFILIATION: Department of Biochemistry, Boston University School of Medicine, MA 02118, USA.

Country: UNITED STATES

AGENCY: United States NIDDK

GRANT: DK 44619

ACRONYM: DK

MEDLINETA: J Dent Res

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