Topic
Yeast
About: Yeast is a research topic. Over the lifetime, 31777 publications have been published within this topic receiving 868967 citations. The topic is also known as: yeasts.
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TL;DR: The in vitro yeast tubulin assembly is inhibited by the fungicide methyl N-(benzimidazol-2-yl)carbamate, the active component of benomyl, whereas in vitro brain 6S tubulinAssembly is resistant, which suggests that the inhibitory effect of Benomyl on yeast cell division is due to its antimicrotubule action.
Abstract: Tubulin was purified from yeast homogenate by DEAE-Sephadex column chromatography and temperature-dependent assembly. The yeast tubulin subunits comigrate with the brain alpha-tubulin subunit on one-dimensional sodium dodecyl sulfate gel electrophoresis. The in vitro yeast tubulin assembly is inhibited by the fungicide methyl N-(benzimidazol-2-yl)carbamate, the active component of benomyl, whereas in vitro brain 6S tubulin assembly is resistant. This suggests that the inhibitory effect of benomyl on yeast cell division is due to its antimicrotubule action.
185 citations
TL;DR: It is reported that yeast Hst2p and a mammalian Hst 2p homologue, hSirT2p, are cytoplasmic in yeast and human cells, in contrast to yHst1p and ySir2p which are exclusively nuclear.
Abstract: In budding yeast, the silent information regulator Sir2p is a nuclear NAD-dependent deacetylase that is essential for both telomeric and rDNA silencing. All eukaryotic species examined to date have multiple homologues of Sir two (HSTs), which share a highly conserved globular core domain. Here we report that yeast Hst2p and a mammalian Hst2p homologue, hSirT2p, are cytoplasmic in yeast and human cells, in contrast to yHst1p and ySir2p which are exclusively nuclear. Although yHst2p cannot restore silencing in a sir2 deletion, overexpression of yHst2p influences nuclear silencing events in a SIR2 strain, derepressing subtelomeric silencing while increasing repression in the rDNA. In contrast, a form of ySir2p carrying a point mutation in the conserved core domain disrupts both telomeric position effect (TPE) and rDNA repression at low expression levels. This argues that non-nuclear yHst2p can compete for a substrate or ligand specifically required for telomeric, and not rDNA repression.
185 citations
TL;DR: These results provide evidence for different substrate specificities of m-AAA proteases composed of different subunits and reveal a striking evolutionary switch of proteases involved in the proteolytic processing of dynamin-like GTPases in mitochondria.
Abstract: The morphology of mitochondria in mammalian cells is regulated by proteolytic cleavage of OPA1, a dynamin-like GTPase of the mitochondrial inner membrane. The mitochondrial rhomboid protease PARL, and paraplegin, a subunit of the ATP-dependent m-AAA protease, were proposed to be involved in this process. Here, we characterized individual OPA1 isoforms by mass spectrometry, and we reconstituted their processing in yeast to identify proteases involved in OPA1 cleavage. The yeast homologue of OPA1, Mgm1, was processed both by PARL and its yeast homologue Pcp1. Neither of these rhomboid proteases cleaved OPA1. The formation of small OPA1 isoforms was impaired in yeast cells lacking the m-AAA protease subunits Yta10 and Yta12 and was restored upon expression of murine or human m-AAA proteases. OPA1 processing depended on the subunit composition of mammalian m-AAA proteases. Homo-oligomeric m-AAA protease complexes composed of murine Afg3l1, Afg3l2, or human AFG3L2 subunits cleaved OPA1 with higher efficiency than paraplegin-containing m-AAA proteases. OPA1 processing proceeded normally in murine cell lines lacking paraplegin or PARL. Our results provide evidence for different substrate specificities of m-AAA proteases composed of different subunits and reveal a striking evolutionary switch of proteases involved in the proteolytic processing of dynamin-like GTPases in mitochondria.
185 citations
TL;DR: The study has revealed ten invariant residues and a number of highly conserved residues present in peroxidases of the plantPeroxidase superfamily and provides a basis for rationally engineered peroxIDases.
185 citations
TL;DR: The approach described in this review will enable us to endow living cells, including yeast cells, with novel additional abilities and to open new dimensions in the field of biotechnology.
185 citations