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Role of BMH proteins in the regulation of yeast enzyme neutral trehalase

Project goals

The overall goal of this project is tounderstand the structural basis of BMH–dependent regulation of the activity ofthe enzyme Neutral trehalase (NTH1). Site-directed mutagenesis, steady-statefluorescence spectroscopy, time-resolved fluorescence spectroscopy, X-raycrystallography, analytical ultracentrifugation and enzyme kineticsmeasurements will be the principal tools. NTH1 is responsible for trehalosedegradation and is required in a variety stress conditions. Activity of theNTH1 enzyme was just recently found to be mediated by BMH1 and BMH2 binding inyeast. The role of yeast BMH proteins in the regulation of NTH1 seems toincreasethe enzymatic activity of the NTH1 enzyme. However details concerninginteraction between the BMH proteins and NTH1 remain still unknown. Sincetrehalose metabolism is an essential component of the stress response inyeastcells, thus, the elucidation of the mechanisms of NTH1 protein regulation,which is still unresolved, would provide us with important informationconcerning mechanisms of both the 14-3-3 protein function and the regulation ofthe neutral trehalase activity in yeast.

Keywords

14-3-3proteinneutraltrehalasefluorescenceactivityassayproteincrystallography

Public support

  • Provider

    Czech Science Foundation

  • Programme

    Standard projects

  • Call for proposals

    Standardní projekty 14 (SGA02011GA-ST)

  • Main participants

    Fyziologický ústav AV ČR, v. v. i.

  • Contest type

    VS - Public tender

  • Contract ID

    P207-11-0455

Alternative language

  • Project name in Czech

    Úloha BMH proteinů v regulaci kvasničného enzymu neutrální trehalásy

  • Annotation in Czech

    Hlavním cílem tohoto projektu je porozumění strukturní podstaty regulace aktivity enzymu neutrální trehalasy (NTH1) prostřednictvím vazby BMH proteinů. Hlavními metodami budou cílená mutageneze, stacionární a časově rozlišená fluorescenční spektroskopie, proteinová krystalografie, analytická ultracentrifugace a studium enzymové kinetiky. NTH1 je zodpovědná za degradaci trehalosy a je vyžadována v řadě stresových situací. Nedávno bylo zjištěno, že aktivita enzymu NTH1 je v kvasinkách regulována vazbou BMH proteinů. Úloha kvasničných BMH proteinů v regulaci NTH1 se zdá být zvyšování enzymové aktivity NTH1 enzymu. Avšak detaily týkající se interakce mezi BMH proteiny a NTH1 stále zůstávají neobjasněny. Poněvadž metabolismus trehalosy je základní složkou odpovědi na stres v buňkách kvasinek, objasnění mechanismů regulace aktivity NTH1, které je stále nevyřešeno, nám poskytne velmi důležitou informaci týkající se mechanismu jak funkce 14-3-3 proteinu, tak i regulace aktivity neutrální trehalasy v kvasinkách.

Scientific branches

  • R&D category

    ZV - Basic research

  • CEP classification - main branch

    CE - Biochemistry

  • CEP - secondary branch

    BO - Biophysics

  • CEP - another secondary branch

  • 10608 - Biochemistry and molecular biology
    10609 - Biochemical research methods
    10610 - Biophysics

Completed project evaluation

  • Provider evaluation

    U - Uspěl podle zadání (s publikovanými či patentovanými výsledky atd.)

  • Project results evaluation

    The planned objectives were met. The grant project significantly contributed to the characterization of yeast enzyme neutral trehalase. In addition, two new binding sites with the molecule of Nth1 were indentified. The obtained results were published in a high-level journals.

Solution timeline

  • Realization period - beginning

    Jan 1, 2011

  • Realization period - end

    Dec 31, 2015

  • Project status

    U - Finished project

  • Latest support payment

    Mar 26, 2015

Data delivery to CEP

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

  • Data delivery code

    CEP16-GA0-GA-U/01:1

  • Data delivery date

    Sep 25, 2017

Finance

  • Total approved costs

    5,975 thou. CZK

  • Public financial support

    5,975 thou. CZK

  • Other public sources

    0 thou. CZK

  • Non public and foreign sources

    0 thou. CZK

Basic information

Recognised costs

5 975 CZK thou.

Public support

5 975 CZK thou.

100%


Provider

Czech Science Foundation

CEP

CE - Biochemistry

Solution period

01. 01. 2011 - 31. 12. 2015