Dockerin-like sequences in cellulases and xylanases from the rumen cellulolytic bacterium Ruminococcus flavefaciens

J Kirby, J C Martin, A S Daniel, H J Flint

Research output: Contribution to journalArticle

54 Citations (Scopus)

Abstract

Recent analysis of the endA cellulase gene from Ruminococcus flavefaciens 17 has revealed that it encodes a product of 759 amino acids that provides the first example of a multidomain cellulase from a Ruminococcus sp. Following the family 5 catalytic domain in the predicted EndA enzyme is a 282 amino acid domain of unknown function for which no close relationship was found to other protein sequences. However, the C-terminal sequences of EndA contain a 34 amino acid threonine-rich linker connected to an 81 amino acid region, both of which show strong similarities to sequences present in two xylanases from ii. flavefaciens 17. A distant relationship is evident between regions of the 80 amino acid sequences of EndA, XynD and XynB and the duplicated 23 amino acid dockerin sequences found in cellulolytic Clostridium sp., suggesting that as in Clostridium sp. these sequences could mediate the binding of enzymatic polypeptides to another component in the cell surface enzyme complex of R. flavefaciens.

Original languageEnglish
Pages (from-to)213-219
Number of pages7
JournalFEMS Microbiology Letters
Volume149
Issue number2
Publication statusPublished - 15 Apr 1997

Keywords

  • Ruminococcus flavefaciens
  • dockerin
  • cellulase
  • xylanase
  • domain organization
  • multienzyme complex
  • cellulosome
  • rumen bacteria
  • CELL-SURFACE-STRUCTURES
  • ENDO-1,4-BETA-GLUCANASE GENE
  • DNA-SEQUENCE
  • DOMAINS
  • ALBUS
  • IDENTIFICATION
  • ENDOGLUCANASE
  • DEGRADATION
  • CLOSTRIDIUM
  • CLONING

Cite this

Dockerin-like sequences in cellulases and xylanases from the rumen cellulolytic bacterium Ruminococcus flavefaciens. / Kirby, J ; Martin, J C ; Daniel, A S ; Flint, H J .

In: FEMS Microbiology Letters, Vol. 149, No. 2, 15.04.1997, p. 213-219.

Research output: Contribution to journalArticle

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KW - CLONING

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JO - FEMS Microbiology Letters

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