The functional repertoire of prokaryote cellulosomes includes the serpin superfamily of serine proteinase inhibitors

Seungha Kang, Yoav Barak, Raphael Lamed, Edward A. Bayer, Mark Morrison*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

Abstract

Many of the Firmicutes bacteria responsible for plant polysaccharide degradation in Nature produce a multiprotein complex called a cellulosome, which co-ordinates glycoside hydrolase assembly, bacterial adhesion to substrate and polysaccharide hydrolysis. Cellulosomal proteins possess a dockerin module, which mediates their attachment to the scaffoldin protein via its interaction with cohesin modules, and only glycoside hydrolases and other carbohydrate active enzymes were known to reside within the cellulosome. We show here with Clostridium thermocellum ATCC 27405 that members of the serpin superfamily of serine proteinase inhibitors, which are best recognized for their conformational flexibility and co-ordination of key regulatory functions in multicellular eukaryotes, also reside within the cellulosome. These studies are the first to expand the cellulosome paradigm of protein complex assembly beyond glycoside hydrolase and carbohydrate active enzymes, and to include a newly identified functionality in the Firmicutes.

Original languageEnglish
Pages (from-to)1344-1354
Number of pages11
JournalMolecular Microbiology
Volume60
Issue number6
DOIs
StatePublished - Jun 2006

Fingerprint

Dive into the research topics of 'The functional repertoire of prokaryote cellulosomes includes the serpin superfamily of serine proteinase inhibitors'. Together they form a unique fingerprint.

Cite this