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The modular xylanase Xyn10A from Rhodothermus marinus is cell-attached, and its C-terminal domain has several putative homologues among cell-attached proteins within the phylum Bacteroidetes

Nordberg Karlsson, Eva LU ; Abou-Hachem, Maher LU ; Ramchuran, Santosh LU ; Costa, Hugo; Holst, Olle LU ; Fex Svenningsen, Åsa LU and Hreggvidsson, Gudmundur O (2004) In FEMS Microbiology Letters 241(2). p.233-242
Abstract
Until recently, the function of the fifth domain of the thermostable modular xylanase Xyn10A from Rhodothermus marinus was unresolved. A putative homologue to this domain was however identified in a mannanase (Man26A) from the same microorganism which raised questions regarding a common function. An extensive search of all accessible data-bases as well as the partially sequenced genomes of R. marinus and Cytophaga hutchinsonii showed that homologues of this domain were encoded by multiple genes in microorganisms in the phylum Bacteroidetes. Moreover, the domain occurred invariably at the C-termini of proteins that were predominantly extra-cellular/cell attached. A primary structure motif of three conserved regions including structurally... (More)
Until recently, the function of the fifth domain of the thermostable modular xylanase Xyn10A from Rhodothermus marinus was unresolved. A putative homologue to this domain was however identified in a mannanase (Man26A) from the same microorganism which raised questions regarding a common function. An extensive search of all accessible data-bases as well as the partially sequenced genomes of R. marinus and Cytophaga hutchinsonii showed that homologues of this domain were encoded by multiple genes in microorganisms in the phylum Bacteroidetes. Moreover, the domain occurred invariably at the C-termini of proteins that were predominantly extra-cellular/cell attached. A primary structure motif of three conserved regions including structurally important glycines and a proline was also identified suggesting a conserved 3D fold. This bioinformatic evidence suggested a possible role of this domain in mediating cell attachment. To confirm this theory, R. marinus was grown, and activity assays showed that the major part of the xylanase activity was connected to whole cells. Moreover, immunocytochemical detection using a Xyn10A-specific antibody proved presence of Xyn10A on the R. marinus cell surface. In the light of this, a revision of experimental data present on both Xyn10A and Man26A was performed, and the results all indicate a cell-anchoring role of the domain, suggesting that this domain represents a novel type of module that mediates cell attachment in proteins originating from members of the phylum Bacteroidetes. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Cell attachment, Xylanase, Bacteroidetes
in
FEMS Microbiology Letters
volume
241
issue
2
pages
233 - 242
publisher
Elsevier
external identifiers
  • wos:000226174000016
  • pmid:15598538
  • scopus:10444265893
ISSN
1574-6968
DOI
10.1016/j.femsle.2004.10.026
language
English
LU publication?
yes
id
7902540b-d248-4c2d-8481-22a46455eafc (old id 141660)
alternative location
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=15598538&query_hl=87
date added to LUP
2007-06-26 11:33:10
date last changed
2017-12-10 04:26:02
@article{7902540b-d248-4c2d-8481-22a46455eafc,
  abstract     = {Until recently, the function of the fifth domain of the thermostable modular xylanase Xyn10A from Rhodothermus marinus was unresolved. A putative homologue to this domain was however identified in a mannanase (Man26A) from the same microorganism which raised questions regarding a common function. An extensive search of all accessible data-bases as well as the partially sequenced genomes of R. marinus and Cytophaga hutchinsonii showed that homologues of this domain were encoded by multiple genes in microorganisms in the phylum Bacteroidetes. Moreover, the domain occurred invariably at the C-termini of proteins that were predominantly extra-cellular/cell attached. A primary structure motif of three conserved regions including structurally important glycines and a proline was also identified suggesting a conserved 3D fold. This bioinformatic evidence suggested a possible role of this domain in mediating cell attachment. To confirm this theory, R. marinus was grown, and activity assays showed that the major part of the xylanase activity was connected to whole cells. Moreover, immunocytochemical detection using a Xyn10A-specific antibody proved presence of Xyn10A on the R. marinus cell surface. In the light of this, a revision of experimental data present on both Xyn10A and Man26A was performed, and the results all indicate a cell-anchoring role of the domain, suggesting that this domain represents a novel type of module that mediates cell attachment in proteins originating from members of the phylum Bacteroidetes.},
  author       = {Nordberg Karlsson, Eva and Abou-Hachem, Maher and Ramchuran, Santosh and Costa, Hugo and Holst, Olle and Fex Svenningsen, Åsa and Hreggvidsson, Gudmundur O},
  issn         = {1574-6968},
  keyword      = {Cell attachment,Xylanase,Bacteroidetes},
  language     = {eng},
  number       = {2},
  pages        = {233--242},
  publisher    = {Elsevier},
  series       = {FEMS Microbiology Letters},
  title        = {The modular xylanase Xyn10A from Rhodothermus marinus is cell-attached, and its C-terminal domain has several putative homologues among cell-attached proteins within the phylum Bacteroidetes},
  url          = {http://dx.doi.org/10.1016/j.femsle.2004.10.026},
  volume       = {241},
  year         = {2004},
}