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Literature summary for 3.6.5.2 extracted from

  • Kang, C.H.; Park, J.H.; Lee, E.S.; Paeng, S.K.; Chae, H.B.; Chi, Y.H.; Lee, S.Y.
    Exploring novel functions of the small GTPase Ypt1p under heat-shock by characterizing a temperature-sensitive mutant yeast strain, ypt1-G80D (2019), Int. J. Mol. Sci., 20, 132 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.6.5.2

Activating Compound

Activating Compound Comment Organism Structure
guanine nucleotide exchange factor Ypt1p requires guanine nucleotide exchange factor for the GDP-GTP exchange and subsequent activation of the signaling process Saccharomyces cerevisiae
additional information GTPase-activating proteins are required for hydrolysis of the bound GTP Saccharomyces cerevisiae

Cloned(Commentary)

Cloned (Comment) Organism
gene YPT1, recombinant expression of GST-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)pLysS Saccharomyces cerevisiae

Protein Variants

Protein Variants Comment Organism
G80D the Ypt1pG80D mutant protein has normal GTPase function and the ypt1-G80D mutant strain displays normal growth and nearly normal endoplasmic reticulum-to-Golgi vesicle trafficking at typical growth temperature (30°C), but experiences growth retardation at an elevated temperature (37°C). Ypt1pG80D does not undergo a heat-shock-induced structural change in vivo. Ypt1pG80D loses molecular chaperone activity. Sodium 4-phenylbutyric acid (PBA), a chemical chaperone, increases the thermotolerance of mutant ypt1-G80D cells, although it is not restored to the level seen for the wild-type YPT1 strain Saccharomyces cerevisiae

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
GTP + H2O Saccharomyces cerevisiae
-
 GDP + phosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant GST-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3)pLysS by glutathione affinity chromatography, the GST-tag is removed by thrombin cleavage, followed by heparin affinity chromatography, DnaK removal by ATP affinity chromatography, and dialysis Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
GTP + H2O
-
 Saccharomyces cerevisiae GDP + phosphate
-
 ?

Synonyms

Synonyms Comment Organism
small GTPase
-
 Saccharomyces cerevisiae
Ypt1
-
 Saccharomyces cerevisiae
Ypt1p
-
 Saccharomyces cerevisiae

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Saccharomyces cerevisiae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Saccharomyces cerevisiae

General Information

General Information Comment Organism
evolution Ypt1p is a member of the Rab family of small GTPases. A large number of small GTPases belonging to the Rab family play a role in vesicular trafficking Saccharomyces cerevisiae
malfunction temperature-sensitive growth phenotype of the ypt1-G80D mutant strain. Complete knockout of the YPT1 gene in yeast is lethal. Abrogation of heat-shock-induced Ypt1p chaperone function by the G80D mutation lowers cell viability largely by hindering metabolism and cellular energy generation. Mutant Ypt1pG80D retains GTPase activity but loses molecular chaperone activity Saccharomyces cerevisiae
metabolism identification of diverse putative Ypt1p-regulatory proteins under heat-shock, overview Saccharomyces cerevisiae
additional information Ypt1p cycles between an active GTP-bound form and an inactive GDP-bound form. Native-PAGE analysis confirms that heat-shock treatment induces the reversible formation of high-molecular-weight protein complexes containing Ypt1p in vivo Saccharomyces cerevisiae
physiological function Ypt1p, a Rab family small GTPase protein, exhibits a stress-driven structural and functional switch from a GTPase to a molecular chaperone, and mediates thermo tolerance in Saccharomyces cerevisiae. The enzyme Ypt1p has another function in addition to its well-known GTPase function, which is temperature-dependent and promotes the survival and growth of cells under heat-stress. The GTPase activity of Ypt1p is not essential for the growth of yeast at elevated temperatures. Ypt1p controls an abundance of proteins involved in metabolism, protein synthesis, cellular energy generation, stress response, and DNA regulation. Ypt1p is essential for multiple steps of the yeast secretory pathway, including endoplasmic reticulum to cis-Golgi and cis- to medial-Golgi transport. Ypt1p essentially regulates fundamental cellular processes under heat-stress conditions by acting as a molecular chaperone Saccharomyces cerevisiae