Molecular and General Genetics MGG

, Volume 252, Issue 4, pp 493–496

Characterization of genes fromThermoanaerobacterium thermosulfurigenes EM1 that encode two glycosyl hydrolases with conserved S-layer-like domains

  • M. Matuschek
  • K. Sahm
  • A. Zibat
  • H. Bahl
Short Communication

Abstract

Two genes fromThermoanaerobacterium thermosulfurigenes EM1 were identified which are predicted to encode a xylanase (XynA) and a polygalacturonate hydrolase (PglA). ThexynA gene has the potential to encode a 1234-amino acid product consisting of a signal peptide followed by a repeated domain, a xylanase family F domain, two cellulose-binding domains and a triplicated sequence at its C-terminus. The genepglA is predicted to encode a product of 1148 amino acids consisting of a signal sequence followed by a fibronectin type III-like domain (Fn3 domain), the catalytic domain, a Gly/Thr/Ser/Asn-rich segment and a triplicated domain. The triplicated segments at the C-termini of deduced XynA and PglA are about 95% identical to each other and to the S-layer-like domains of the previously characterized pullulanase (AmyB) from the same organism. In contrast, sequence comparisons revealed only distant amino acid sequence similarities between the fibronectin type III-like domains of PglA and AmyB fromT. thermosulfurigenes EM1.

Key words

Pullulanase Xylanase Polygalacturonate hydrolase S-layer Thermophilic bacteria 

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Copyright information

© Springer-Verlag 1996

Authors and Affiliations

  • M. Matuschek
    • 1
  • K. Sahm
    • 1
  • A. Zibat
    • 1
  • H. Bahl
    • 1
  1. 1.Institut für MikrobiologieGeorg-August-Universität GöttingenGöttingenGermany
  2. 2.Max-Planck-Institut für Marine MikrobiologieBremenGermany
  3. 3.Institut für Molekulare GenetikGeorg-August-Universität GöttingenGöttingenGermany
  4. 4.Universität Rostock, Fachbereich Biologie, MikrobiologieRostockGermany

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