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

KRE2  -  alpha-1,2-mannosyltransferase KRE2

Saccharomyces cerevisiae S288c

Synonyms: Alpha-1,2-mannosyltransferase, D8035.26, Glycolipid 2-alpha-mannosyltransferase, MNT1, YDR483W
 
 
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.
 

High impact information on KRE2

  • However, in a test of targeting sufficiency, the presence of the entire Kre2p cytoplasmic tail, plus the transmembrane domain and a 36-amino acid residue luminal stem region was required to localize a Pho8p reporter protein to the yeast Golgi [1].
  • Anti-Kre2p/Mnt1p antibodies identify a 60-kD integral membrane protein that is progressively N-glycosylated in an MNN1-dependent manner [1].
  • Kre2p/Mnt1p is localized in a Golgi compartment that overlaps with that containing the medial-Golgi mannosyltransferase Mnn1p, and distinct from that including the late Golgi protein Kex1p [1].
  • The results demonstrate that the NH2-terminal cytoplasmic domain is necessary for correct Kre2p Golgi localization whereas, the membrane-spanning and stem domains are dispensable [1].
  • Mnt1p is an alpha 1.2-mannosyltransferase which resides in an early compartment of the Saccharomyces cerevisiae Golgi apparatus [2].
 

Biological context of KRE2

  • In order to better define how such post-translational modifications occur, we have been studying a yeast gene family in which at least one member, KRE2/MNT1, is involved in protein glycosylation [3].
  • The KRE2 gene is close to PHO8 on chromosome 4, and encodes a predicted 49-kD protein, Kre2p, that probably enters the secretory pathway [4].
  • Haploid cells carrying a disruption of the KRE2 locus grow more slowly than wild-type cells at 30 degrees, and fail to grow at 37 degrees [4].
  • In addition, MNT1 is part of a multigene family whose members are presumed to be yeast Golgi mannosyltransferases [5].
  • Gene fusions encoding the membrane anchor region of yeast alpha1, 2-mannosyltransferase (Mnt1p) fused to human beta1, 4-galactosyltransferase (Gal-Tf) were constructed and expressed in the yeast Saccharomyces cerevisiae [6].
 

Anatomical context of KRE2

 

Associations of KRE2 with chemical compounds

  • In contrast to KRE2 null mutants, which produce shortened (two-mannose) chains, mutants harboring a KTR2 gene disruption synthesize O-linked chains with the wild-type patterns of five mannose residues [9].
  • Determination of the mobility of the specifically N-linked glycoprotein invertase in different null strains indicates that Ktr1p, Ktr3p, and Kre2p are also jointly involved in N-linked glycosylation, possibly in establishing some of the outer chain alpha1,2-linkages [10].
  • After induction with methanol, the medium contained approx, 40 and 400 mg/l of soluble recombinant Kre2p/Mnt1p and Ktr1p respectively [11].
  • Null mutants of MNT1 are viable, have no apparent growth defect, and are blocked in the elongation of protein O-linked mannobiose [5].
  • A final Golgi localization of both fusions was confirmed by sucrose gradient fractionations, in which Gal-Tf activity cofractionated with Golgi Mnt1p activity, as well as by immunocytological localization experiments using a monoclonal anti-Gal-Tf antibody [6].
 

Co-localisations of KRE2

  • However, no defect in vacuolar acidification is apparent from quinacrine staining, and Gef1p co-localizes with Mnt1p in the medial Golgi [12].
 

Regulatory relationships of KRE2

 

Other interactions of KRE2

  • Yur1p has an N-terminal signal sequence like Kre2p, while Ktr1p has a predicted topology consistent with a type 2 membrane protein [4].
  • KTR2: a new member of the KRE2 mannosyltransferase gene family [9].
  • Nucleotide sequence analysis of an 11.7 kb fragment of yeast chromosome II including BEM1, a new gene of the WD-40 repeat family and a new member of the KRE2/MNT1 family [14].
  • To demonstrate in vivo activity of the Mnt1/Gal-Tf fusion the encoding plasmids were transformed in an alg1 mutant, which at the non-permissive temperature transfers short (GlcNAc)2 glycosyl chains to proteins [6].
  • The glaA gene encoding glucoamylase I (GAI) of Aspergillus awamori var. kawachi was heterologously expressed in mannosyltransferase mutants of Saccharomyces cerevisiae, in which the pmt1 gene and the kre2 gene were disrupted [15].

References

  1. Localization and targeting of the Saccharomyces cerevisiae Kre2p/Mnt1p alpha 1,2-mannosyltransferase to a medial-Golgi compartment. Lussier, M., Sdicu, A.M., Ketela, T., Bussey, H. J. Cell Biol. (1995) [Pubmed]
  2. The functioning of the yeast Golgi apparatus requires an ER protein encoded by ANP1, a member of a new family of genes affecting the secretory pathway. Chapman, R.E., Munro, S. EMBO J. (1994) [Pubmed]
  3. Functional characterization of the YUR1, KTR1, and KTR2 genes as members of the yeast KRE2/MNT1 mannosyltransferase gene family. Lussier, M., Sdicu, A.M., Camirand, A., Bussey, H. J. Biol. Chem. (1996) [Pubmed]
  4. Yeast KRE2 defines a new gene family encoding probable secretory proteins, and is required for the correct N-glycosylation of proteins. Hill, K., Boone, C., Goebl, M., Puccia, R., Sdicu, A.M., Bussey, H. Genetics (1992) [Pubmed]
  5. Yeast glycoprotein biosynthesis: MNT1 encodes an alpha-1,2-mannosyltransferase involved in O-glycosylation. Häusler, A., Ballou, L., Ballou, C.E., Robbins, P.W. Proc. Natl. Acad. Sci. U.S.A. (1992) [Pubmed]
  6. Golgi localization and in vivo activity of a mammalian glycosyltransferase (human beta1,4-galactosyltransferase) in yeast. Schwientek, T., Narimatsu, H., Ernst, J.F. J. Biol. Chem. (1996) [Pubmed]
  7. Topography of glycosylation in yeast: characterization of GDPmannose transport and lumenal guanosine diphosphatase activities in Golgi-like vesicles. Abeijon, C., Orlean, P., Robbins, P.W., Hirschberg, C.B. Proc. Natl. Acad. Sci. U.S.A. (1989) [Pubmed]
  8. Interaction of the endoplasmic reticulum alpha 1,2-mannosidase Mns1p with Rer1p using the split-ubiquitin system. Massaad, M.J., Herscovics, A. J. Cell. Sci. (2001) [Pubmed]
  9. KTR2: a new member of the KRE2 mannosyltransferase gene family. Lussier, M., Camirand, A., Sdicu, A.M., Bussey, H. Yeast (1993) [Pubmed]
  10. The Ktr1p, Ktr3p, and Kre2p/Mnt1p mannosyltransferases participate in the elaboration of yeast O- and N-linked carbohydrate chains. Lussier, M., Sdicu, A.M., Bussereau, F., Jacquet, M., Bussey, H. J. Biol. Chem. (1997) [Pubmed]
  11. Ktr1p is an alpha-1,2-mannosyltransferase of Saccharomyces cerevisiae. Comparison of the enzymic properties of soluble recombinant Ktr1p and Kre2p/Mnt1p produced in Pichia pastoris. Romero, P.A., Lussier, M., Sdicu, A.M., Bussey, H., Herscovics, A. Biochem. J. (1997) [Pubmed]
  12. Golgi localization and functionally important domains in the NH2 and COOH terminus of the yeast CLC putative chloride channel Gef1p. Schwappach, B., Stobrawa, S., Hechenberger, M., Steinmeyer, K., Jentsch, T.J. J. Biol. Chem. (1998) [Pubmed]
  13. MNN5 encodes an iron-regulated alpha-1,2-mannosyltransferase important for protein glycosylation, cell wall integrity, morphogenesis, and virulence in Candida albicans. Bai, C., Xu, X.L., Chan, F.Y., Lee, R.T., Wang, Y. Eukaryotic Cell (2006) [Pubmed]
  14. Nucleotide sequence analysis of an 11.7 kb fragment of yeast chromosome II including BEM1, a new gene of the WD-40 repeat family and a new member of the KRE2/MNT1 family. Mallet, L., Bussereau, F., Jacquet, M. Yeast (1994) [Pubmed]
  15. Functional analysis of O-linked oligosaccharides in threonine/serine-rich region of Aspergillus glucoamylase by expression in mannosyltransferase-disruptants of yeast. Goto, M., Tsukamoto, M., Kwon, I., Ekino, K., Furukawa, K. Eur. J. Biochem. (1999) [Pubmed]
 
WikiGenes - Universities