A scaffoldin of the Bacteroides cellulosolvens cellulosome that contains 11 type II cohesins

被引:57
作者
Ding, SY
Bayer, EA [1 ]
Steiner, D
Shoham, Y
Lamed, R
机构
[1] Weizmann Inst Sci, Dept Biol Chem, IL-76100 Rehovot, Israel
[2] Tel Aviv Univ, Dept Mol Microbiol & Biotechnol, Ramat Aviv, Israel
[3] Technion Israel Inst Technol, Dept Food Engn & Biotechnol, Haifa, Israel
[4] Technion Israel Inst Technol, Inst Catalysis Sci & Technol, Haifa, Israel
关键词
D O I
10.1128/JB.182.17.4915-4925.2000
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
A cellulosomal scaffoldin gene, termed cipBc, was identified and sequenced from the mesophilic cellulolytic anaerobe Bacteroides cellulosolvens, The gene encodes a 2,292-residue polypeptide (excluding the signal sequence) with a calculated molecular weight of 242,437, CipBc contains an N-terminal signal peptide, 11 type II cohesin domains, an internal family III cellulose-binding domain (CBD), and a C-terminal dockerin domain. Its CBD belongs to family IIIb, like that of CipV from Acetivibrio cellulolyticus but unlike the family IIIa CBDs of other clostridial scaffoldins, In contrast to all other scaffoldins thus far described, CipBc lacks a hydrophilic domain or domain X of unknown function. The singularity of CipBc, however, lies in its numerous type II cohesin domains, all of which are very similar in sequence. One of the latter cohesin domains was expressed, and the expressed protein interacted selectively with cellulosomal enzymes, one of which was identified as a family 48 glycosyl hydrolase on the basis of partial sequence alignment. By definition, the dockerins, carried by the cellulosomal enzymes of this species, would be considered to be type II, This is the first example of authentic type II cohesins that are confirmed components of a cellulosomal scaffoldin subunit rather than a cell surface anchoring component, The results attest to the emerging diversity of cellulosomes and their component sequences in nature.
引用
收藏
页码:4915 / 4925
页数:11
相关论文
共 40 条
[11]   NOVEL OLIGOSACCHARIDE CONSTITUENTS OF THE CELLULASE COMPLEX OF BACTEROIDES-CELLULOSOLVENS [J].
GERWIG, GJ ;
KAMERLING, JP ;
VLIEGENTHART, JFG ;
MORAG, E ;
LAMED, R ;
BAYER, EA .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1992, 205 (02) :799-808
[12]  
GERWIG GJ, 1993, J BIOL CHEM, V268, P26956
[13]   CELLULASE AND SUGAR FORMATION BY BACTEROIDES-CELLULOSOLVENS, A NEWLY ISOLATED CELLULOLYTIC ANAEROBE [J].
GIULIANO, C ;
KHAN, AW .
APPLIED AND ENVIRONMENTAL MICROBIOLOGY, 1984, 48 (02) :446-448
[14]   CONVERSION OF CELLULOSE TO SUGARS BY RESTING CELLS OF A MESOPHILIC ANAEROBE, BACTEROIDES-CELLULOSOLVENS [J].
GIULIANO, C ;
KHAN, AW .
BIOTECHNOLOGY AND BIOENGINEERING, 1985, 27 (07) :980-983
[15]   Cloning and DNA sequencing of the genes encoding Clostridium josui scaffolding protein CipA and cellulase CelD and identification of their gene products as major components of the cellulosome [J].
Kakiuchi, M ;
Isui, A ;
Suzuki, K ;
Fujino, T ;
Fujino, E ;
Kimura, T ;
Karita, S ;
Saki, K ;
Ohmiya, K .
JOURNAL OF BACTERIOLOGY, 1998, 180 (16) :4303-4308
[16]  
Lamed R., 1988, Biochemistry and genetics of cellulose degradation, P101
[17]   CELLULOSOME-LIKE ENTITIES IN BACTEROIDES-CELLULOSOLVENS [J].
LAMED, R ;
MORAG, E ;
MORYOSEF, O ;
BAYER, EA .
CURRENT MICROBIOLOGY, 1991, 22 (01) :27-33
[18]   SPECIALIZED CELL-SURFACE STRUCTURES IN CELLULOLYTIC BACTERIA [J].
LAMED, R ;
NAIMARK, J ;
MORGENSTERN, E ;
BAYER, EA .
JOURNAL OF BACTERIOLOGY, 1987, 169 (08) :3792-3800
[19]   THE CELLULOSOME OF CLOSTRIDIUM-THERMOCELLUM [J].
LAMED, R ;
BAYER, EA .
ADVANCES IN APPLIED MICROBIOLOGY, 1988, 33 :1-46
[20]   CHARACTERIZATION OF A CELLULOSE-BINDING, CELLULASE-CONTAINING COMPLEX IN CLOSTRIDIUM-THERMOCELLUM [J].
LAMED, R ;
SETTER, E ;
BAYER, EA .
JOURNAL OF BACTERIOLOGY, 1983, 156 (02) :828-836