High impact information on STM1

• The yeast STM1 gene encodes a purine motif triple helical DNA-binding protein [1].
• MPT4 was isolated in a screen for multicopy suppressors of staurosporine sensitivity in POP2 cells [2].
• STO1 was isolated as a multicopy suppressor of TOM1, an uncharacterized mutation that leads to temperature-sensitive cell cycle arrest at the G2/M boundary [2].
• Suppression of these mutations by G4p2 indicate this G4 nucleic acid binding protein may function in signal transduction pathways regulated by protein kinases, which control carbon source utilization, and in cell cycle progression [2].
• Two of these associated proteins, Mpt4p and Asc1p, were nearly stoichiometrically bound to the ribosome [3].

Biological context of STM1

• STM1 has been implicated in the control of apoptosis, and indeed, this work shows that disruption of this gene results, among other phenotypes, in resistance to aging [4].
• A new gene (STM1; suppressor of tom1) of Saccharomyces cerevisiae was isolated by the ability to suppress the temperature sensitivity of a tom1 mutant, by increasing its gene dosage [5].
• Partial amino acid sequence of AF was determined from its fragment of 25 kDa isolated by treating AF with 2-(2-nitrophenylsulfenyl)-3-methyl-3'-Bromoindolenine (BNPS-skatole) [6].

Regulatory relationships of STM1

• A high dose of the STM1 gene suppresses the temperature sensitivity of the tom1 and htr1 mutants in Saccharomyces cerevisiae [5].

Analytical, diagnostic and therapeutic context of STM1

• Confirmation that Stm1p is a purine motif triplex-binding protein was obtained by electrophoretic mobility shift assays using either bacterially expressed, recombinant Stm1p or whole-cell extracts from stm1Delta yeast [1].

References