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
Sequences	Protein DNA Advanced_DNA
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

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)