Regulation of Sulfur Metabolism in Cephalosporium acremonium

Cephalosporium acremonium에서 황화합물 대사의 조절

  • Lee, Kyoung (Genetic Engineering Center, Korea Advanced Institute of science and Technology) ;
  • Park, Sang-Ho (Genetic Engineering Center, Korea Advanced Institute of science and Technology) ;
  • Lee, Jung-Joon (Genetic Engineering Center, Korea Advanced Institute of science and Technology) ;
  • Mheen, Tae-Ick (Genetic Engineering Center, Korea Advanced Institute of science and Technology)
  • Published : 1987.10.01

Abstract

A DL-seleno-methionine resistant mutant, Cephalosporium acremonium MS-92 showed increased activities of sulfate and L-methionine uptake than the parent strain, and accumulated excess methionine and S-adenosylmethionine (SAM) intracellularly. And the sulfate uptake system was severely inhibited by L-cysteine. In crude enzyme extracts, the mutant MS-92 showed lower L-serine sulfhydrylase (identical with cystathionine $\beta$-synthase) activity than the parent. Also, cysteine desulfhydrylase activity, an index of intracellular L-cysteine concentration, of the mutant MS-92 was decreased by about 50% as com-pared with that of the parent. Thus, it was supposed that the mutant MS-92 should have n lower level of L-cysteine than the parent. In C. acremonium like A. nidulans, the enzymes related to the biosynthesis of methionine might be regulated by L-cysteine, but not by methionine or SAM.

DL-seleno-methionine에 내성을 갖는 변이주, Cephalosporium acremonium MS-92는 무기황과 메치오닌의 Uptake rate가 모균보다 우수하였으며, 세포내에 과량의 메치오닌과 S-adenosylmethionine (SAM)을 축적하였다. 또 C. acremonium에서 무기황의 uptake rate는 시스테인에 의해 크게 저해되었다. Crude enzymes extracts에서 변이주 MS-92 는 cell내에 cysteine을 적게 형성하였다 즉, L.-serine sulfhydrylase 활성이 모균보다 낮았으며 세포내에 시스테인의 양을 간접적으로 알 수 있는 시스테인 분해효소인 cysteine desulfhydrylase 활성치 변이주에는 모균의 약 반이였다. 이상의 결과에서 C. acremonium에서 메치오닌을 만드는 효소들의 조절에는 A. nidulans와 비슷하게 시스테인이 관여한다는 것을 추측할 수 있었다.

Keywords