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A conserved NAD+ binding pocket that regulates protein-protein interactions during aging

Title data

Li, Jun ; Bonkowski, Michael S. ; Moniot, Sébastien ; Zhang, Dapeng ; Hubbard, Basil P. ; Ling, Alvin J. Y. ; Rajman, Luis A. ; Qin, Bo ; Lou, Zhenkun ; Gorbunova, Vera ; Aravind, L. ; Steegborn, Clemens ; Sinclair, David A.:
A conserved NAD+ binding pocket that regulates protein-protein interactions during aging.
In: Science. Vol. 355 (24 March 2017) Issue 6331 . - pp. 1312-1317.
ISSN 1095-9203
DOI: https://doi.org/10.1126/science.aad8242

Abstract in another language

DNA repair is essential for life, yet its efficiency declines with age for reasons that are unclear. Numerous proteins possess Nudix homology domains (NHDs) that have no known function. We show that NHDs are NAD(+) (oxidized form of nicotinamide adenine dinucleotide) binding domains that regulate protein-protein interactions. The binding of NAD(+) to the NHD domain of DBC1 (deleted in breast cancer 1) prevents it from inhibiting PARP1 [poly(adenosine diphosphate-ribose) polymerase], a critical DNA repair protein. As mice age and NAD(+) concentrations decline, DBC1 is increasingly bound to PARP1, causing DNA damage to accumulate, a process rapidly reversed by restoring the abundance of NAD(+) Thus, NAD(+) directly regulates protein-protein interactions, the modulation of which may protect against cancer, radiation, and aging.

Further data

Item Type: Article in a journal
Refereed: Yes
Institutions of the University: Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biochemistry > Chair Biochemistry - Univ.-Prof. Dr. Clemens Steegborn
Faculties
Faculties > Faculty of Biology, Chemistry and Earth Sciences
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biochemistry
Result of work at the UBT: No
DDC Subjects: 500 Science > 540 Chemistry
Date Deposited: 29 Mar 2017 06:49
Last Modified: 28 Mar 2022 09:30
URI: https://eref.uni-bayreuth.de/id/eprint/36681