INTERACTION BETWEEN THE ENDOGLUCANASE CELA AND THE SCAFFOLDING PROTEIN CIPC OF THE CLOSTRIDIUM CELLULOLYTICUM CELLULOSOME
作者： S Pagès , A Belaich , C Tardif , C Reverbel-Leroy , C Gaudin
DOI: 10.1128/JB.178.8.2279-2286.1996
关键词: Cohesin 、 N-terminus 、 Biology 、 Cohesin domain 、 Dockerin 、 Clostridium cellulolyticum 、 Cellulosome 、 Peptide sequence 、 Cellulosome assembly 、 Biochemistry
摘要: The 5' end of the cipC gene, coding for N-terminal part CipC, scaffolding protein Clostridium cellulolyticum ATCC 35319, was cloned and sequenced. It encodes a 586-amino-acid peptide, including several domains: cellulose-binding domain, hydrophilic two hydrophobic domains (cohesin domains). Sequence alignments showed that N terminus CipC CbpA C. cellulovorans 35296 have same organization. mini-CipC polypeptide, containing domain 1, cohesin overexpressed in Escherichia coli purified. interaction between endoglucanase CelA, with (CelA2) without (CelA3) characteristic clostridial C-terminal called duplicated-segment or dockerin polypeptide monitored by different methods: Western blotting (immunoblotting) method binding assays biotin-labeled protein. Among various forms CelA (CelA2, CelA3, an intermediary form only duplicated segment), CelA2 found to interact 1 CipC. apparent equilibrium dissociation constant CelA2-mini-CipC complex 7 x 10(-9)M, which indicates there exists high affinity these proteins.
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