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.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

Links

 

Gene Review

OASA1  -  O-acetylserine (thiol) lyase (OAS-TL)...

Arabidopsis thaliana

Synonyms: ATCYS-3A, CYTACS1, DL3480C, FCAALL.34, O-ACETHYLSERINE SULFHYDRYLASE, ...
 
 
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 OASA1

 

High impact information on OASA1

  • Comparison with bacterial OASS suggests that structural plasticity in the active site allows binding of SAT C termini with dissimilar sequences at structurally similar OASS active sites [2].
  • In plants, association of O-acetylserine sulfhydrylase (OASS) and Ser acetyltransferase (SAT) into the Cys synthase complex plays a regulatory role in sulfur assimilation and Cys biosynthesis [2].
  • In addition, examination of the AtOASS structure and nearly 300 plant and bacterial OASS sequences suggest that the highly conserved beta8A-beta9A surface loop may be important for interaction with serine acetyltransferase, the other enzyme in cysteine biosynthesis [3].
  • O-Acetylserine sulfhydrylase (OASS) catalyzes the final step of cysteine biosynthesis, the pyridoxal 5'-phosphate (PLP)-dependent conversion of O-acetylserine into cysteine [3].
  • Both effector concentrations are in the range of intracellular O-acetylserine fluctuations and support a functional model that integrates effector-driven cysteine synthase complex dissociation as a regulatory switch for the biosynthetic pathway [4].
 

Biological context of OASA1

  • Expression of wild-type OASA1 or OASA2 transgenes did not affect the Trp content of rice calli or plants [5].
  • A DNA regulatory fragment was isolated from the promoter region of the OASA1 gene, encoding the cytosolic O-acetylserine(thiol)lyase enzyme that is highly expressed in Arabidopsis thaliana trichomes [6].
  • The cDNA for cysteine synthase encodes an open reading frame of 325 amino acids, of which expression in the E. coli lacking endogenous cysteine synthase genes could functionally rescue the growth without addition of cysteine [7].
 

Associations of OASA1 with chemical compounds

  • Molecular basis of cysteine biosynthesis in plants: structural and functional analysis of O-acetylserine sulfhydrylase from Arabidopsis thaliana [3].
  • Although the plant and bacterial OASS share a conserved set of amino acids for PLP binding, the structure of AtOASS reveals a difference from the bacterial enzyme in the positioning of an active site loop formed by residues 74-78 when methionine is bound [3].
  • However, transformed calli and plants expressing a mutated OASA1 gene, OASA1(D323N), that encodes a protein in which aspartate-323 is replaced with asparagine manifested up to 180- and 35-fold increases, respectively, in Trp accumulation [5].
  • Characterization of rice anthranilate synthase alpha-subunit genes OASA1 and OASA2. Tryptophan accumulation in transgenic rice expressing a feedback-insensitive mutant of OASA1 [5].
  • beta-Cyanoalanine synthase is a mitochondrial cysteine synthase-like protein in spinach and Arabidopsis [8].
 

Analytical, diagnostic and therapeutic context of OASA1

  • Molecular cloning and expression analyses of mitochondrial and plastidic isoforms of cysteine synthase (O-acetylserine(thiol)lyase) from Arabidopsis thaliana [9].

References

  1. Genomic and functional characterization of the oas gene family encoding O-acetylserine (thiol) lyases, enzymes catalyzing the final step in cysteine biosynthesis in Arabidopsis thaliana. Jost, R., Berkowitz, O., Wirtz, M., Hopkins, L., Hawkesford, M.J., Hell, R. Gene (2000) [Pubmed]
  2. Structural basis for interaction of o-acetylserine sulfhydrylase and serine acetyltransferase in the Arabidopsis cysteine synthase complex. Francois, J.A., Kumaran, S., Jez, J.M. Plant Cell (2006) [Pubmed]
  3. Molecular basis of cysteine biosynthesis in plants: structural and functional analysis of O-acetylserine sulfhydrylase from Arabidopsis thaliana. Bonner, E.R., Cahoon, R.E., Knapke, S.M., Jez, J.M. J. Biol. Chem. (2005) [Pubmed]
  4. Use of biomolecular interaction analysis to elucidate the regulatory mechanism of the cysteine synthase complex from Arabidopsis thaliana. Berkowitz, O., Wirtz, M., Wolf, A., Kuhlmann, J., Hell, R. J. Biol. Chem. (2002) [Pubmed]
  5. Characterization of rice anthranilate synthase alpha-subunit genes OASA1 and OASA2. Tryptophan accumulation in transgenic rice expressing a feedback-insensitive mutant of OASA1. Tozawa, Y., Hasegawa, H., Terakawa, T., Wakasa, K. Plant Physiol. (2001) [Pubmed]
  6. A versatile promoter for the expression of proteins in glandular and non-glandular trichomes from a variety of plants. Gutiérrez-Alcalá, G., Calo, L., Gros, F., Caissard, J.C., Gotor, C., Romero, L.C. J. Exp. Bot. (2005) [Pubmed]
  7. Molecular cloning and functional characterization of cDNAs encoding cysteine synthase and serine acetyltransferase that may be responsible for high cellular cysteine content in Allium tuberosum. Urano, Y., Manabe, T., Noji, M., Saito, K. Gene (2000) [Pubmed]
  8. beta-Cyanoalanine synthase is a mitochondrial cysteine synthase-like protein in spinach and Arabidopsis. Hatzfeld, Y., Maruyama, A., Schmidt, A., Noji, M., Ishizawa, K., Saito, K. Plant Physiol. (2000) [Pubmed]
  9. Molecular cloning and expression analyses of mitochondrial and plastidic isoforms of cysteine synthase (O-acetylserine(thiol)lyase) from Arabidopsis thaliana. Hesse, H., Lipke, J., Altmann, T., Höfgen, R. Amino Acids (1999) [Pubmed]
 
WikiGenes - Universities