Current Microbiology

, Volume 27, Issue 1, pp 27–33

Analyses of the gene and amino acid sequence of thePrevotella (bacteroides) ruminicola 23 xylanase reveals unexpected homology with endoglucanases from other genera of bacteria

  • Terence R. Whitehead
Article

DOI: 10.1007/BF01576830

Cite this article as:
Whitehead, T.R. Current Microbiology (1993) 27: 27. doi:10.1007/BF01576830

Abstract

The DNA sequence for the xylanase gene fromPrevotella (Bacteroides) ruminicola 23 was determined. The xylanase gene encoded for a protein with a molecular weight of 65,740. An apparent leader sequence of 22 amino acids was observed. The promoter region for expression of the xylanase gene inBacteroides species was identified with a promoterless chloramphenicol acetyltransferase gene. A region of high amino acid homology was found with the proposed catalytic domain of endoglucanases from several organisms, includingButyrivibrio fibrisolvens, Ruminococcus flavefaciens, andClostridium thermocellum. The cloned xylanase was found to exhibit endoglucanase activity against carboxymethyl cellulose. Analysis of the codon usage for the xylanase gene found a bias towards G and C in the third position in 16 of 18 amino acids with degenerate codons.

Copyright information

© Springer-Verlag New York Inc. 1993

Authors and Affiliations

  • Terence R. Whitehead
    • 1
  1. 1.Fermentation Biochemistry Research, National Center for Agricultural Utilization ResearchUnited States Department of Agriculture, Agricultural Research ServicePeoriaUSA

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