HPF1 dynamically controls the PARP1/2 balance between initiating and elongating ADP-ribose modifications

Autor: Marie-France Langelier, Ramya Billur, Aleksandr Sverzhinsky, Ben E. Black, John M. Pascal

Publikováno v: Nature Communications, Vol 12, Iss 1, Pp 1-14 (2021)

HPF1 controls the ADP-ribosylation activity of PARP1/2 in response to DNA breaks. Here, the authors show that HPF1 regulates the balance between ADP-ribose initiation and elongation through a dynamic interaction that accelerates the initiation rate o

Externí odkaz: https://doaj.org/article/6078d4725d6843d48dcd1bc9e7b93b53

An atypical BRCT-BRCT interaction with the XRCC1 scaffold protein compacts human DNA Ligase IIIα within a flexible DNA repair complex

Autor: John A. Tainer, Miaw Sheue Tsai, In-Kwon Kim, Michal Hammel, Ishtiaque Rashid, Aleksandr Sverzhinsky, John M. Pascal, Yasin Pourfarjam, Tom Ellenberger, Alan E. Tomkinson

Publikováno v: Nucleic acids research, vol 49, iss 1
Nucleic Acids Research

The XRCC1–DNA ligase IIIα complex (XL) is critical for DNA single-strand break repair, a key target for PARP inhibitors in cancer cells deficient in homologous recombination. Here, we combined biophysical approaches to gain insights into the shape

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6ba641c041cec3209c7d5e05d086461a
https://escholarship.org/uc/item/9q41p570

Cryo-EM structures and biochemical insights into heterotrimeric PCNA regulation of DNA ligase

Autor: John M. Pascal, Alan E. Tomkinson, Aleksandr Sverzhinsky

Publikováno v: Structure

DNA ligases act in the final step of many DNA repair pathways and are commonly regulated by the DNA sliding clamp proliferating cell nuclear antigen (PCNA), but there are limited insights into the physical basis for this regulation. Here, we use sing

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3c4c20713f1570d728bb14ea797f2007
https://doi.org/10.1016/j.str.2021.11.002

VirB8 homolog TraE from plasmid pKM101 forms a hexameric ring structure and interacts with the VirB6 homolog TraD

Autor: Charline Mary, Antonio Nanci, Aurélien Fouillen, Bastien Casu, Aleksandr Sverzhinsky, Christian Baron

Publikováno v: Proceedings of the National Academy of Sciences of the United States of America. 115(23)

Type IV secretion systems (T4SSs) are multiprotein assemblies that translocate macromolecules across the cell envelope of bacteria. X-ray crystallographic and electron microscopy (EM) analyses have increasingly provided structural information on indi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::df81989b6a4bbe89be6c79ab6f9d7c8a
https://pubmed.ncbi.nlm.nih.gov/29784815

Amphipol-Trapped ExbB–ExbD Membrane Protein Complex from Escherichia coli: A Biochemical and Structural Case Study

Autor: Jacqueline W. Chung, Jean-Luc Popot, Lin Yang, James W. Coulton, Aleksandr Sverzhinsky, Isabel Moraes, Marc Allaire, Dewang Ma, Manuela Zoonens, Shuo Qian

Publikováno v: Journal of Membrane Biology
Journal of Membrane Biology, Springer Verlag (Germany), 2014, 247 (9-10), pp.1005-1018. ⟨10.1007/s00232-014-9678-4⟩

Nutrient import across Gram-negative bacte- ria's outer membrane is powered by the proton-motive force, delivered by the cytoplasmic membrane protein complex ExbB-ExbD-TonB. Having purified the ExbB4- ExbD2 complex in the detergent dodecyl maltoside,

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::248713adfc5b7f9cf86adecda99439db
https://doi.org/10.1007/s00232-014-9678-4