Difference between revisions of "YoaJ"

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[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 10:48, 21 September 2012

  • 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:
  • Interactions:
  • Localization: extracellular PubMed

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

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)

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)

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)