YoaJ

• 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 This image was kindly provided by SubtiList
Expression at a glance   PubMed

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]

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

• Structure: 3D3O PubMed

• UniProt: O34918

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: yoaJ PubMed

• Expression browser: yoaJ PubMed

• Sigma factor:

• Regulation:
  • induced upon iron starvation (Fur) PubMed

• Regulatory mechanism:
  • Fur: transcription repression PubMed

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

In Jung Kim, Hyeok-Jin Ko, Tae-Wan Kim, In-Geol Choi, Kyoung Heon Kim
Characteristics of the binding of a bacterial expansin (BsEXLX1) to microcrystalline cellulose.
Biotechnol Bioeng: 2013, 110(2);401-7
[PubMed:22949138] [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)