Affiliation:
1. Faculty of Bioresources1 and
2. Nagoya Seiraku Co., Ltd., Nagoya 468,2 Japan
3. Center for Molecular Biology and Genetics,3 Mie University, Tsu 514, and
Abstract
ABSTRACT
The
Clostridium josui cipA
and
celD
genes, encoding a scaffolding-like protein (CipA) and a putative cellulase (CelD), respectively, have been cloned and sequenced. CipA, with an estimated molecular weight of 120,227, consists of an N-terminal signal peptide, a cellulose-binding domain of family III, and six successive cohesin domains. The molecular architecture of
C. josui
CipA is similar to those of the scaffolding proteins reported so far, such as
Clostridium thermocellum
CipA,
Clostridium cellulovorans
CbpA, and
Clostridium cellulolyticum
CipC, but
C. josui
CipA is considerably smaller than the other scaffolding proteins. CelD consists of an N-terminal signal peptide, a family 48 catalytic domain of glycosyl hydrolase, and a dockerin domain. N-terminal amino acid sequence analysis of the
C. josui
cellulosomal proteins indicates that both CipA and CelD are major components of the cellulosome.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
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