Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Editor

Personal info

View

About

Terms

Javascript disabled

Please enable Javascript support in your browser to use this application.

Instructions on how to enable JavaScript on different browsers can be found here: http://www.google.com/support/bin/answer.py?answer=23852.

[edit this page]

Gene Review:

MBP2 - myrosinase-binding protein 2

Arabidopsis thaliana

Synonyms: F-ATMBP, F5F19.9, F5F19_9, MBP1.2, MYROSINASE BINDING PROTEIN

Capella, A.N. et al., Desikan, R. et al., Novikova, G.V. et al., Yoo, J.H. et al., Berthold, D.A. et al.

Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of MBP2

Elicitation of Arabidopsis thaliana (L.) Heynh. suspension cultures with the bacterial protein harpin (from Pseudomonas syringae pv. syringae) induced the activation of two kinases of 39 and 44 kDa, as demonstrated by in-gel kinase assays using myelin basic protein (MBP) as a substrate [1].
We isolated a mutant vector for MBP fusions that exhibited a more optimal level of expression for complementation of aerobic respiration in hemA(-) E. coli, our functional assay for the alternative oxidase [2].

High impact information on MBP2

At increasing concentrations of CaM, the biochemical activity of dual specificity protein phosphatase 1 on the p-nitrophenyl phosphate (pNPP) substrate was increased, whereas activity on the phosphotyrosine of myelin basic protein (MBP) was inhibited [3].
The cDNAs (MBP1 and MBP2) correspond to two open-reading frames found in a gene cluster of seven putative MBP genes located on chromosome 1 [4].
MBP2 contains a region of high content of proline and alanine residues, commonly found in arabinogalactan proteins and hydroxyproline-rich glycoproteins [4].
Transcripts corresponding to MBP1 and MBP2 genes are exclusively and abundantly expressed in flowers but are not detected in male-sterile flowers of coi1 plants, insensitive to jasmonic acid [4].
The results show that COI1 controls MBP expression in flowers and significantly affects the expression and activity of myrosinase in Arabidopsis [4].

Biological context of MBP2

Treatment of wild type with ethylene resulted in increased myelin basic protein (MBP) phosphorylation [5].

Associations of MBP2 with chemical compounds

Both MAPKinase (ERK 1) and phosphotyrosine antibodies immunoprecipitated MBP-phosphorylating activity and detected a polypeptide band at M(r) approximately 47 kDa [5].

Other interactions of MBP2

The predicted proteins MBP1 and MBP2 are similar to lectins and plant aggregating factors [4].

Analytical, diagnostic and therapeutic context of MBP2

Northern analysis and in situ hybridization revealed that MBP mRNAs are present in higher levels in immature flowers and are localized in several floral organs, including the ovary, ovules, style, anthers and filament [4].

References

Harpin induces mitogen-activated protein kinase activity during defence responses in Arabidopsis thaliana suspension cultures. Desikan, R., Clarke, A., Atherfold, P., Hancock, J.T., Neill, S.J. Planta (1999) [Pubmed]
Screening for functional expression and overexpression of a family of diiron-containing interfacial membrane proteins using the univector recombination system. Berthold, D.A., Stenmark, P., Nordlund, P. Protein Sci. (2003) [Pubmed]
Regulation of the dual specificity protein phosphatase, DsPTP1, through interactions with calmodulin. Yoo, J.H., Cheong, M.S., Park, C.Y., Moon, B.C., Kim, M.C., Kang, Y.H., Park, H.C., Choi, M.S., Lee, J.H., Jung, W.Y., Yoon, H.W., Chung, W.S., Lim, C.O., Lee, S.Y., Cho, M.J. J. Biol. Chem. (2004) [Pubmed]
COI1 affects myrosinase activity and controls the expression of two flower-specific myrosinase-binding protein homologues in Arabidopsis. Capella, A.N., Menossi, M., Arruda, P., Benedetti, C.E. Planta (2001) [Pubmed]
The effect of ethylene on MAPKinase-like activity in Arabidopsis thaliana. Novikova, G.V., Moshkov, I.E., Smith, A.R., Hall, M.A. FEBS Lett. (2000) [Pubmed]

Contributions to this collaborative article are from individual authors of WikiGenes or mined by the WikiGenes Data Mining Engine from MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.About WikiGenes Open Access Licence Privacy Policy Terms of Use apsburg

The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.