Abstract:
:Bacillus brevis 47 contains two cell wall proteins termed the outer wall protein (OWP) and middle wall protein (MWP), each of which forms hexagonal arrays in the cell wall. A 6-kilobase BglII-BclI fragment of B. brevis 47 DNA cloned into Bacillus subtilis with a derivative of pHW1 as a vector directed the synthesis of a polypeptide, with almost the same molecular weight as the authentic OWP, as judged by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, which was specifically recognized by the anti-OWP antibody. Nucleotide sequence analysis of the subfragment revealed that it contains two open reading frames in tandem. The upstream truncated open reading frame corresponds to the carboxy-terminal portion of the MWP, and the downstream open reading frame corresponds to the entire translational portion of the OWP. The latter encodes a secretory precursor of the OWP, consisting of a total of 1,004 amino acid residues with a signal peptide of 24 amino acid residues at its amino-terminal end. Futhermore, analysis of transcripts in B. brevis 47 suggests that the MWP and OWP genes, in that order, constitute a cotranscriptional unit and that the major promoter shared by the two genes is located upstream of the MWP gene.
journal_name
J Bacterioljournal_title
Journal of bacteriologyauthors
Tsuboi A,Uchihi R,Tabata R,Takahashi Y,Hashiba H,Sasaki T,Yamagata H,Tsukagoshi N,Udaka Sdoi
10.1128/jb.168.1.365-373.1986subject
Has Abstractpub_date
1986-10-01 00:00:00pages
365-73issue
1eissn
0021-9193issn
1098-5530journal_volume
168pub_type
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更新日期:2002-01-01 00:00:00