YoaJ

From SubtiWiki
Revision as of 18:31, 14 October 2012 by Jstuelk (talk | contribs)
Jump to: navigation, search
  • Description: bacterial expansin, binds cellulose, required for the colonization of maize roots

Gene name yoaJ
Synonyms
Essential no
Product expansin
Function interaction with plant roots
Gene expression levels in SubtiExpress: yoaJ
MW, pI 25 kDa, 9.447
Gene length, protein length 696 bp, 232 aa
Immediate neighbours yoaI, yoaK
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
YoaJ context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
YoaJ expression.png















Categories containing this gene/protein

lifestyles/ miscellaneous

This gene is a member of the following regulons

Fur regulon

The gene

Basic information

  • Locus tag: BSU18630

Phenotypes of a mutant

strongly reduced ability to colonize maize roots PubMed

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family: expansin PubMed
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Sigma factor:
  • Regulation:
  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Additional publications: PubMed

In Jung Kim, Hyeok-Jin Ko, Tae-Wan Kim, Ki Hyun Nam, In-Geol Choi, Kyoung Heon Kim
Binding characteristics of a bacterial expansin (BsEXLX1) for various types of pretreated lignocellulose.
Appl Microbiol Biotechnol: 2013, 97(12);5381-8
[PubMed:23053073] [WorldCat.org] [DOI] (I p)

Nikolaos Georgelis, Neela H Yennawar, Daniel J Cosgrove
Structural basis for entropy-driven cellulose binding by a type-A cellulose-binding module (CBM) and bacterial expansin.
Proc Natl Acad Sci U S A: 2012, 109(37);14830-5
[PubMed:22927418] [WorldCat.org] [DOI] (I p)

Nikolaos Georgelis, Akira Tabuchi, Nikolas Nikolaidis, Daniel J Cosgrove
Structure-function analysis of the bacterial expansin EXLX1.
J Biol Chem: 2011, 286(19);16814-23
[PubMed:21454649] [WorldCat.org] [DOI] (I p)

Eun Sil Kim, Hee Jin Lee, Won-Gi Bang, In-Geol Choi, Kyoung Heon Kim
Functional characterization of a bacterial expansin from Bacillus subtilis for enhanced enzymatic hydrolysis of cellulose.
Biotechnol Bioeng: 2009, 102(5);1342-53
[PubMed:19058186] [WorldCat.org] [DOI] (I p)

Frédéric Kerff, Ana Amoroso, Raphaël Herman, Eric Sauvage, Stéphanie Petrella, Patrice Filée, Paulette Charlier, Bernard Joris, Akira Tabuchi, Nikolas Nikolaidis, Daniel J Cosgrove
Crystal structure and activity of Bacillus subtilis YoaJ (EXLX1), a bacterial expansin that promotes root colonization.
Proc Natl Acad Sci U S A: 2008, 105(44);16876-81
[PubMed:18971341] [WorldCat.org] [DOI] (I p)

Neela H Yennawar, Lian-Chao Li, David M Dudzinski, Akira Tabuchi, Daniel J Cosgrove
Crystal structure and activities of EXPB1 (Zea m 1), a beta-expansin and group-1 pollen allergen from maize.
Proc Natl Acad Sci U S A: 2006, 103(40);14664-71
[PubMed:16984999] [WorldCat.org] [DOI] (P p)

Hans Kende, Kent Bradford, David Brummell, Hyung-Taeg Cho, Daniel Cosgrove, Andrew Fleming, Chris Gehring, Yi Lee, Simon McQueen-Mason, Jocelyn Rose, Laurentius A C J Voesenek
Nomenclature for members of the expansin superfamily of genes and proteins.
Plant Mol Biol: 2004, 55(3);311-4
[PubMed:15604683] [WorldCat.org] [DOI] (P p)

Noel Baichoo, Tao Wang, Rick Ye, John D Helmann
Global analysis of the Bacillus subtilis Fur regulon and the iron starvation stimulon.
Mol Microbiol: 2002, 45(6);1613-29
[PubMed:12354229] [WorldCat.org] [DOI] (P p)