ompT对重组波形蛋白的截短。鉴定III型中间丝蛋白组装所必需的头部结构域中的一个短基序。

Truncation of recombinant vimentin by ompT. Identification of a short motif in the head domain necessary for assembly of type III intermediate filament proteins.

作者信息

Hatzfeld M, Dodemont H, Plessmann U, Weber K

机构信息

Max Planck Institute for Biophysical Chemistry, Department of Biochemistry, Goettingen, Germany.

出版信息

FEBS Lett. 1992 May 18;302(3):239-42. doi: 10.1016/0014-5793(92)80450-u.

DOI:10.1016/0014-5793(92)80450-u

PMID:1601131

Abstract

Recombinant vimentin expressed in E. coli JM 101 cells is cleaved after cell lysis between arginines 11 and 12. The truncated vimentin is assembly incompetent. Expression of the same cDNA construct in BL21 cells, which lack the protease ompT, provides intact and polymerization-competent vimentin. The ompT cleavage site is contained in a short sequence motif (YRRMF) shared by the head domains of type III and IV intermediate filament (IF) proteins. We propose that a related motif present in the N-terminal 32 residues of lambda CII accounts for the known IF formation of a fusion protein formed with a truncated GFAP.

摘要

在大肠杆菌JM 101细胞中表达的重组波形蛋白在细胞裂解后于精氨酸11和12之间被切割。截短的波形蛋白无组装能力。在缺乏蛋白酶ompT的BL21细胞中表达相同的cDNA构建体，可提供完整且具有聚合能力的波形蛋白。ompT切割位点包含在III型和IV型中间丝（IF）蛋白头部结构域共有的短序列基序（YRRMF）中。我们提出，λ CII N端32个残基中存在的一个相关基序解释了与截短的GFAP形成的融合蛋白已知的IF形成情况。