Prof. Dr. Ann Ehrenhofer-Murray
Profil
Zusammenfassung
Ann Ehrenhofer-Murray erforscht die chemischen Modifikationen von RNA und Histonen sowie deren Rolle bei grundlegenden Zellprozessen wie Transkription, DNA-Replikation und Chromosomenstabilität. Sie entwickelt Methoden zur Analyse dieser Modifikationen und untersucht, wie sie die Genexpression und Zellfunktion regulieren — Erkenntnisse, die für die Entwicklung von Therapeutika und für das Verständnis von Krankheitsmechanismen relevant sind.
Skills
Stammdaten
Identität, Organisation und Kontakt aus HU-FIS.
Forschungsthemen15
Analyse der Interaktion der AAA+ Domäne des Heterochromatin-Protein Sir3
Quelle ↗Förderer: DFG Sachbeihilfe Zeitraum: 10/2013 - 08/2018 Projektleitung: Prof. Dr. Ann Ehrenhofer-Murray
Characterization of the Dnmt2 methyltransferase homolog pmt1 from Schizosaccharomyces pombe
Quelle ↗Förderer: DFG Sachbeihilfe Zeitraum: 08/2013 - 07/2016 Projektleitung: Prof. Dr. Ann Ehrenhofer-Murray, Martin Müller
Characterization of the role of serine phosphorylation on CenH3 function in Saccharomyces cerevisiae
Quelle ↗Förderer: DFG Sachbeihilfe Zeitraum: 10/2013 - 08/2019 Projektleitung: Prof. Dr. Ann Ehrenhofer-Murray
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Publikationen25
Top 25 nach Zitationen — Quelle: OpenAlex (BAAI/bge-m3 embedded für Matching).
European Journal of Biochemistry · 290 Zitationen · DOI
During DNA replication, transcription and DNA repair in eukaryotes, the cellular machineries performing these tasks need to gain access to the DNA that is packaged into chromatin in the nucleus. Chromatin is a dynamic structure that modulates the access of regulatory factors to the genetic material. A precise coordination and organization of events in opening and closing of the chromatin is crucial to ensure that the correct spatial and temporal epigenetic code is maintained within the eukaryotic genome. This review will summarize the current knowledge of how chromatin remodeling and histone modifying complexes cooperate to break and remake chromatin during nuclear processes on the DNA template.
Molecular and Cellular Biology · 226 Zitationen · DOI
The majority of cytosolic proteins in eukaryotes contain a covalently linked acetyl moiety at their very N terminus. The mechanism by which the acetyl moiety is efficiently transferred to a large variety of nascent polypeptides is currently only poorly understood. Yeast N(alpha)-acetyltransferase NatA, consisting of the known subunits Nat1p and the catalytically active Ard1p, recognizes a wide range of sequences and is thought to act cotranslationally. We found that NatA was quantitatively bound to ribosomes via Nat1p and contained a previously unrecognized third subunit, the N(alpha)-acetyltransferase homologue Nat5p. Nat1p not only anchored Ard1p and Nat5p to the ribosome but also was in close proximity to nascent polypeptides, independent of whether they were substrates for N(alpha)-acetylation or not. Besides Nat1p, NAC (nascent polypeptide-associated complex) and the Hsp70 homologue Ssb1/2p interact with a variety of nascent polypeptides on the yeast ribosome. A direct comparison revealed that Nat1p required longer nascent polypeptides for interaction than NAC and Ssb1/2p. Delta nat1 or Delta ard1 deletion strains were temperature sensitive and showed derepression of silent mating type loci while Delta nat5 did not display any obvious phenotype. Temperature sensitivity and derepression of silent mating type loci caused by Delta nat1 or Delta ard1 were partially suppressed by overexpression of SSB1. The combination of data suggests that Nat1p presents the N termini of nascent polypeptides for acetylation and might serve additional roles during protein synthesis.
RNA Biology · 223 Zitationen · DOI
A group of homologous nucleic acid modification enzymes called Dnmt2, Trdmt1, Pmt1, DnmA, and Ehmet in different model organisms catalyze the transfer of a methyl group from the cofactor S-adenosyl-methionine (SAM) to the carbon-5 of cytosine residues. Originally considered as DNA MTases, these enzymes were shown to be tRNA methyltransferases about a decade ago. Between the presumed involvement in DNA modification-related epigenetics, and the recent foray into the RNA modification field, significant progress has characterized Dnmt2-related research. Here, we review this progress in its diverse facets including molecular evolution, structural biology, biochemistry, chemical biology, cell biology and epigenetics.
Kooperationen0
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