Nuclear PIP2 and myosin I: new important players in DNA transcription

Kód výsledku v IS VaVaI

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Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

Nuclear PIP2 and myosin I: new important players in DNA transcription

Popis výsledku v původním jazyce

Nuclear myosin I (NM1) is a 120 kDa molecular motor described in the cell nucleus. NM1 was shown to be involved in chromatin remodeling, repositioning of transcriptionally activated regions and also in transcription with RNA pol I. Myosin 1C binds to negatively charged phospholipids, specifically to phosphatidylinositol-(4,5)bisphosphate (PIP2) and this binding tethers myosin I to plasma membrane. Based on this we asked if NM1 also has binding properties to PIP2. We made single-point mutations in the pleckstrin homology (PH) domain of NM1 and applied fluorescence recovery after photobleaching (FRAP) and fluorescence correlation spectroscopy (FCS). Mutant NM1 became faster in mobility compared to its wild type NM1. We then depleted  PIP2 in the nucleusby co-transfecting the cells with inositol 5-phosphatase. After PIP2 depletion in nuclei, NM1 became faster showing once more that PIP2 binding reduces NM1 mobility. Phospholipase C delta (PLC?) is an enzyme which binds to PIP2 via its PH

Název v anglickém jazyce

Nuclear PIP2 and myosin I: new important players in DNA transcription

Popis výsledku anglicky

Nuclear myosin I (NM1) is a 120 kDa molecular motor described in the cell nucleus. NM1 was shown to be involved in chromatin remodeling, repositioning of transcriptionally activated regions and also in transcription with RNA pol I. Myosin 1C binds to negatively charged phospholipids, specifically to phosphatidylinositol-(4,5)bisphosphate (PIP2) and this binding tethers myosin I to plasma membrane. Based on this we asked if NM1 also has binding properties to PIP2. We made single-point mutations in the pleckstrin homology (PH) domain of NM1 and applied fluorescence recovery after photobleaching (FRAP) and fluorescence correlation spectroscopy (FCS). Mutant NM1 became faster in mobility compared to its wild type NM1. We then depleted  PIP2 in the nucleusby co-transfecting the cells with inositol 5-phosphatase. After PIP2 depletion in nuclei, NM1 became faster showing once more that PIP2 binding reduces NM1 mobility. Phospholipase C delta (PLC?) is an enzyme which binds to PIP2 via its PH

Druh

D - Stať ve sborníku

CEP obor

EB - Genetika a molekulární biologie

OECD FORD obor

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Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

Z - Vyzkumny zamer (s odkazem do CEZ)<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2012

Kód důvěrnosti údajů

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

Název statě ve sborníku

emc2012 manchester, european microscopy congress

ISBN

978-0-9502463-7-6

ISSN

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e-ISSN

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Počet stran výsledku

1

Strana od-do

77-77

Název nakladatele

RMS, IFSM

Místo vydání

Manchester

Místo konání akce

Manchester

Datum konání akce

16. 9. 2012

Typ akce podle státní příslušnosti

EUR - Evropská akce

Kód UT WoS článku

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