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

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...

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Bibliographic Details
Published in:Protein science 2004-05, Vol.13 (5), p.1422-1425
Main Authors: Howard, Michael B., Ekborg, Nathan A., Taylor, Larry E., Hutcheson, Steven W., Weiner, Ronald M.
Format: Article
Language:English
Subjects:
Alteromonadaceae - enzymology
Alteromonadaceae - genetics
Amino Acid Sequence
Bacterial Proteins - chemistry
Bacterial Proteins - genetics
Cellulase - chemistry
Cellulase - genetics
domain linkers
extracellular depolymerases
For the Record
marine bacterium 2–40
microbulbifer degradans
Molecular Sequence Data
Oceans and Seas
Peptides - chemistry
Peptides - genetics
polyserine linker
Protein Structure, Tertiary
secreted carbohydrases
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Summary: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.
ISSN:0961-8368
1469-896X
DOI:10.1110/ps.03511604