Peter B. Becker

ORCID: 0000-0001-7186-0372
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About
Contact & Profiles
Research Areas
  • Genomics and Chromatin Dynamics
  • RNA Research and Splicing
  • Epigenetics and DNA Methylation
  • Chromosomal and Genetic Variations
  • RNA and protein synthesis mechanisms
  • RNA modifications and cancer
  • Protein Degradation and Inhibitors
  • CRISPR and Genetic Engineering
  • Genetic and Clinical Aspects of Sex Determination and Chromosomal Abnormalities
  • Cancer-related gene regulation
  • DNA Repair Mechanisms
  • Ubiquitin and proteasome pathways
  • Chromatin Remodeling and Cancer
  • Insect Resistance and Genetics
  • Histone Deacetylase Inhibitors Research
  • Cancer-related molecular mechanisms research
  • Advanced biosensing and bioanalysis techniques
  • Genetics, Bioinformatics, and Biomedical Research
  • Plant Molecular Biology Research
  • Microtubule and mitosis dynamics
  • Heat shock proteins research
  • RNA Interference and Gene Delivery
  • DNA and Nucleic Acid Chemistry
  • Estrogen and related hormone effects
  • Molecular Biology Techniques and Applications

Ludwig-Maximilians-Universität München
2016-2025

Urologische Klinik München
2019-2023

Center for Integrated Protein Science Munich
2010-2019

Novo Nordisk (Denmark)
2007-2016

University of Birmingham
2007

University of Cambridge
2004

European Molecular Biology Laboratory
1993-2003

European Bioinformatics Institute
1997-2001

Universitäts Frauenklinik
2000

Biologie Labor
2000

Dosage compensation in Drosophila involves a 2-fold increase transcription from the single male X relative to two female chromosomes. Regulation at level of chromosome alterations chromatin organization: chromosomes appear decondensed and are marked by acetylation histone H4 lysine 16. We demonstrate that MOF, protein required for dosage with significant sequence similarity MYST family acetyltransferases, is acetyltransferase acetylates specifically This relieves chromatin-mediated...

10.1016/s1097-2765(00)80431-1 article EN cc-by-nc-nd Molecular Cell 2000-02-01

Using in vivo dimethylsulfate footprinting, we have analyzed protein-DNA interactions within two regions upstream of the tyrosine aminotransferase (TAT) gene that are characterized by an altered chromatin structure TAT-expressing as compared to nonexpressing cells. All identified protein contacts DNA found exclusively hepatoma In vitro analyses specific DNA-binding factors crude nuclear extracts yield DNAase I footprints correlate well with binding sites vivo. Surprisingly, all activities...

10.1016/0092-8674(87)90639-8 article EN cc-by-nc-nd Cell 1987-11-01

Abstract The basic helix–loop–helix (bHLH) family of transcription factors recognizes DNA motifs known as E-boxes (CANNTG) and includes 108 members 1 . Here we investigate how chromatinized are engaged by two structurally diverse bHLH proteins: the proto-oncogene MYC-MAX circadian factor CLOCK-BMAL1 (refs. 2,3 ). Both bind to preferentially near nucleosomal entry–exit sites. Structural studies with engineered or native nucleosome sequences show that triggers release from histones gain...

10.1038/s41586-023-06282-3 article EN cc-by Nature 2023-07-05

The chromatin accessibility complex (CHRAC) belongs to the class of nucleosome remodeling factors that increase nucleosomal DNA in an ATP-dependent manner. We found CHRAC induces movements intact histone octamers neighboring segments without facilitating their displacement competing or chaperones trans. CHRAC-induced energy-dependent sliding may, principle, explain remodeling, positioning, and spacing reactions known be catalyzed by CHRAC. catalytic core CHRAC, ATPase ISWI, also mobilized...

10.1016/s0092-8674(00)80797-7 article EN cc-by-nc-nd Cell 1999-06-01

Sensing DNA damage is crucial for the maintenance of genomic integrity and cell cycle progression. The participation chromatin in these events becoming increasing interest. We show that presence single-strand breaks gaps, formed either directly or during processing, can trigger propagation nucleosomal arrays. This nucleosome assembly pathway involves histone chaperone factor 1 (CAF-1). largest subunit (p150) this interacts with proliferating nuclear antigen (PCNA), critical regions...

10.1128/mcb.20.4.1206-1218.2000 article EN Molecular and Cellular Biology 2000-02-01

The ATPase ISWI is a subunit of several distinct nucleosome remodeling complexes that increase the accessibility DNA in chromatin. We found isolated protein itself was able to carry out remodeling, rearrangement, and chromatin assembly reactions. activity stimulated by nucleosomes but not free or histones, indicating recognizes specific structural feature nucleosomes. Nucleosome therefore, does require functional interaction between other subunits complexes. role proteins associated with may...

10.1016/s1097-2765(00)80314-7 article EN cc-by-nc-nd Molecular Cell 1999-02-01

The ATPase ISWI can be considered the catalytic core of several multiprotein nucleosome remodeling machines.Alone or in context factor, chromatin accessibility complex (CHRAC), ACF, catalyzes a number ATP-dependent transitions structure that are currently best explained by its ability to induce sliding.In addition, function as spacing factor during assembly, where it will trigger ordering newly assembled nucleosomes into regular arrays.Both and reactions mechanistically unexplained.As step...

10.1128/mcb.21.3.875-883.2001 article EN Molecular and Cellular Biology 2001-02-01

We describe a cell-free system, derived from preblastoderm Drosophila embryos, for the efficient assembly of cloned DNA into chromatin. The chromatin system utilizes endogenous core histones and factors yields long arrays regularly spaced nucleosomes with repeat length 180 bp. is also capable complementary-strand synthesis accompanied by rapid nucleosome formation when starting template single-stranded circular DNA. Chromatin assembled embryo extract naturally deficient in histone H1, but...

10.1128/mcb.12.5.2241 article EN Molecular and Cellular Biology 1992-05-01
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