Literature DB >> 18720489

The surface layer protein of Bacillus thuringiensis CTC forms unique intracellular parasporal inclusion body.

Chenguang Zhu1, Ziniu Yu.   

Abstract

Bacillus thuringiensis subsp. finitimus strain CTC forms round parasporal inclusion body. The inclusion body protein gene ctc has been cloned and characterized. Sequence homology analysis reveals that the amino acid sequence of CTC protein shows 87% identity with the surface layer (S-layer) protein Sap (GenBank Z36946) in B. anthracis. In this report, transmission electron microscope observation showed that CTC formed intracellular parasporal inclusion body and sheet structure of S-layer-like protein at the spore phase. Furthermore, the ctc gene was transformed into an acrystalliferous B. thuringiensis strain BMB171. The resulting transformant could form parasporal body which had the same shape and molecular weight of protein with that of B. thuringiensis CTC. These results, together with the sequence homology analysis of ctc gene, confirmed that the unique intracellular parasporal inclusion body of B. thuringiensis was comprised of S-layer protein. (c) 2008 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

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Year:  2008        PMID: 18720489     DOI: 10.1002/jobm.200800013

Source DB:  PubMed          Journal:  J Basic Microbiol        ISSN: 0233-111X            Impact factor:   2.281


  2 in total

Review 1.  Towards revealing the structure of bacterial inclusion bodies.

Authors:  Lei Wang
Journal:  Prion       Date:  2009-07-25       Impact factor: 3.931

2.  Complete genome sequence of Bacillus thuringiensis mutant strain BMB171.

Authors:  Jin He; Xiaohu Shao; Huajun Zheng; Mingshun Li; Jieping Wang; Qingye Zhang; Lin Li; Ziduo Liu; Ming Sun; Shengyue Wang; Ziniu Yu
Journal:  J Bacteriol       Date:  2010-06-04       Impact factor: 3.490

  2 in total

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