Identification and cloning of yeast phosphofructokinase 2
نویسندگان
چکیده
منابع مشابه
Phosphofructokinase Mutants of Yeast
Mutants of Saccharomyces cerevisiae completely lacking the soluble glycolytic enzyme fructose-6-P kinase are described. The mutations are semidominant, do not complement one another, and define a gene PFKl located 28-cm distal to rnal on the extended right arm of chromosome XIII. Of 10 independent mutants, 3 can be suppressed by ochre suppressors. All mutants examined synthesize proteins that c...
متن کاملActivation by phosphate of yeast phosphofructokinase.
The activity of yeast phosphofructokinase assayed in vitro at physiological concentrations of known substrates and effectors is 100-fold lower than the glycolytic flux observed in vivo. Phosphate synergistically with AMP activates the enzyme to a level within the range of the physiological needs. The activation by phosphate is pH-dependent: the activation is 100-fold at pH 6.4 while no effect i...
متن کاملfunctional study of p0 proteins of two cereal yellow dwarf viruses (cydv-rpv and cydv-rps) and identification of their cellular partner
نقش سرکوبگری پروتئین p0 در دو پولروویروس کوتولگی زردی غلات cydv-rpv) و (cydv-rps، متفاوت در شدت بیماریزایی، مورد مطالعه قرار گرفت. نتایج نشان داد که هر دو پروتئین p0 p0cy-rpv) و (p0cy-rps قادر به سرکوب خاموشی آر ان ای ایجاد شده توسط ترادف های تراژن سنس و تکرار معکوس در n. benthamiana هستند. نشان داده شد که هر دو پروتئین p0 می توانند تخریب پروتئین argonaute-1 را تسهیل کنند. علاوه بر این، تمایل م...
Complementation of soluble phosphofructokinase activity in yeast mutants.
We describe here the genetic and biochemical analyses of two classes of mutations in the soluble phosphofructokinase (PFK I) of Saccharomyces cerevisiae: those leading to the loss of activity and those giving rise to a kinetically altered enzyme. Complementation and allele-testing between these two classes of mutants show that loss of enzyme activity in vitro can come about not only by mutation...
متن کاملMutations in the regulatory subunit of soluble phosphofructokinase from yeast.
Mutant alleles of the gene PFK2 have been obtained that alter the sensitivity to ATP inhibition of the soluble yeast phosphofructokinase. One of the alleles makes the enzyme sensitive to micromolar concentrations of ATP. Intragenic revertants of PFK2 mutants confirm that the PFK2 gene determines not only the regulatory properties of the soluble enzyme but also the catalytic activity of particul...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1991
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1991.tb15920.x