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Published online before print April 9, 2004, 10.1110/ps.03511604
Protein Science (2004), 13:1422-1425. Published by Cold Spring Harbor Laboratory Press. Copyright © 2004 The Protein Society
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FOR THE RECORD

Identification and analysis of polyserine linker domains in prokaryotic proteins with emphasis on the marine bacterium Microbulbifer degradans

Michael B. Howard, Nathan A. Ekborg, Larry E. Taylor, Steven W. Hutcheson and Ronald M. Weiner

Department of Cell Biology and Molecular Genetics, University of Maryland, College Park, Maryland 20742, USA

(RECEIVED November 12, 2003; FINAL REVISION December 3, 2003; ACCEPTED December 3, 2003)



Abstract

Polyserine linkers (PSLs) are interdomain, serine-rich sequences found in modular proteins. Though common among eukaryotes, their presence in prokaryotic enzymes is limited. We identified 46 extracellular proteins involved in complex carbohydrate degradation from Microbulbifer degradans that contain PSLs that separate carbohydrate-binding domains or catalytic domains from other binding domains. In nine M. degradans proteins, PSLs also separated amino-terminal lipoprotein acylation sites from the remainder of the polypeptide. Furthermore, among the 76 PSL proteins identified in sequence repositories, 65 are annotated as proteins involved in complex carbohydrate degradation. We discuss the notion that PSLs are flexible, disordered spacer regions that enhance substrate accessibility.

Keywords: microbulbifer degradans; polyserine linker; secreted carbohydrases; domain linkers; marine bacterium 2–40;; extracellular depolymerases

Reprint requests to: Ronald M. Weiner, Department of Cell Biology and Molecular Genetics, University of Maryland, College Park, MD 20742, USA; e-mail: rw19{at}umail.umd.edu; fax: (301) 314-9489

Article published ahead of print. Article and publication date are at http://www.proteinscience.org/cgi/doi/10.1110/ps.03511604.

Supplemental material: see www.proteinscience.org


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