Phenotypic comparison of samdc and spe mutants reveals complex relationships of polyamine metabolism in Ustilago maydis.
Synthesis of spermidine involves the action of two enzymes, spermidine synthase (Spe) and S-adenosylmethionine decarboxylase (Samdc). Previously we cloned and disrupted the gene encoding Spe as a first approach to unravel the biological function of spermidine in Ustilago maydis. With this background, the present study was designed to provide a better understanding of the role played by Samdc in the regulation of the synthesis of this polyamine. With this aim we proceeded to isolate and delete the gene encoding Samdc from U. maydis, and made a comparative analysis of the phenotypes of samdc and spe mutants. Both spe and samdc mutants behaved as spermidine auxotrophs, and were more sensitive than the wild-type strain to different stress conditions. However, the two mutants displayed significant differences: in contrast to spe mutants, samdc mutants were more sensitive to LiCl stress, high spermidine concentrations counteracted their dimorphic deficiency, and they were completely avirulent. It is suggested that these differences are possibly related to differences in exogenous spermidine uptake or the differential location of the respective enzymes in the cell. Alternatively, since samdc mutants accumulate higher levels of S-adenosylmethionine (SAM), whereas spe mutants accumulate decarboxylated SAM, the known opposite roles of these metabolites in the processes of methylation and differentiation offer an additional attractive hypothesis to explain the phenotypic differences of the two mutants, and provide insights into the additional roles of polyamine metabolism in the physiology of the cell.
Departamento de Ingeniería Genética, Unidad Irapuato, Centro de Investigación y de Estudios Avanzados del Instituto Politécnico Nacional, Irapuato, Gto., México.
Laura
L
Valdés-Santiago
Licenciatura en Microbiología, Universidad Autónoma de Querétaro, Querétaro, México.
José Antonio
JA
Cervantes-Chávez
Departamento de Bioquímica y Biotecnología, Unidad Irapuato, Centro de Investigación y de Estudios Avanzados del Instituto Politécnico Nacional, Irapuato, Gto., México.
Robert
R
Winkler
Departamento de Ingeniería Genética, Unidad Irapuato, Centro de Investigación y de Estudios Avanzados del Instituto Politécnico Nacional, Irapuato, Gto., México.
Claudia G
CG
León-Ramírez
Departamento de Ingeniería Genética, Unidad Irapuato, Centro de Investigación y de Estudios Avanzados del Instituto Politécnico Nacional, Irapuato, Gto., México.
José
J
Ruiz-Herrera
D012437:Adenosylmethionine Decarboxylase / Q000235:genetics / Q000378:metabolism*; D004271:DNA, Fungal / Q000737:chemistry / Q000235:genetics; D017353:Gene Deletion; D018021:Lithium Chloride / Q000633:toxicity; D008969:Molecular Sequence Data; D011073:Polyamines / Q000378:metabolism*; D017422:Sequence Analysis, DNA; D011436:Spermidine Synthase / Q000235:genetics / Q000378:metabolism*; D014588:Ustilago / Q000201:enzymology* / Q000235:genetics / Q000254:growth & development / Q000378:metabolism*; D014774:Virulence
D004271:DNA, Fungal; D011073:Polyamines; D011436:Spermidine Synthase; D012437:Adenosylmethionine Decarboxylase; D018021:Lithium Chloride