A single gene directs synthesis of a precursor protein with beta- and alpha-amylase activities in Bacillus polymyxa.

N. Uozumi, K. Sakurai, T. Sasaki, S. Takekawa, H. Yamagata, N. Tsukagoshi, S. Udaka

Research output: Contribution to journalArticle

34 Citations (Scopus)

Abstract

The Bacillus polymyxa amylase gene comprises 3,588 nucleotides. The mature amylase comprises 1,161 amino acids with a molecular weight of 127,314. The gene appeared to be divided into two portions by the direct-repeat sequence located at almost the middle of the gene. The 5' region upstream of the direct-repeat sequence was shown to be responsible for the synthesis of beta-amylase. The 3' region downstream of the direct-repeat sequence contained four sequences homologous with those in other alpha-amylases, such as Taka-amylase A. The 48-kilodalton (kDa) amylase isolated from B. polymyxa was proven to have alpha-amylase activity. The amino acid sequences of the peptides generated from the 48-kDa amylase showed complete agreement with the predicted amino acid sequence of the C-terminal portion. The B. polymyxa amylase gene was therefore concluded to contain in-phase beta- and alpha-amylase-coding sequences in the 5' and 3' regions, respectively. A precursor protein, a 130-kDa amylase, directed by a plasmid, pYN520, carrying the entire amylase gene, had both beta- and alpha-amylase activities. This represents the first report of a single protein precursor in procaryotes that gives rise to two enzymes.

Original languageEnglish
Pages (from-to)375-382
Number of pages8
JournalJournal of bacteriology
Volume171
Issue number1
DOIs
Publication statusPublished - 1989 Jan
Externally publishedYes

ASJC Scopus subject areas

  • Microbiology
  • Molecular Biology

Fingerprint Dive into the research topics of 'A single gene directs synthesis of a precursor protein with beta- and alpha-amylase activities in Bacillus polymyxa.'. Together they form a unique fingerprint.

  • Cite this