Structure and function of the RING domains of RNF20 and RNF40, dimeric E3 ligases that monoubiquitylate histone H2B
Monoubiquitylation of histone H2B is a post-translational mark that plays key roles in
regulation of transcription and genome stability. In humans, attachment of ubiquitin to lysine …
regulation of transcription and genome stability. In humans, attachment of ubiquitin to lysine …
Molecular characterization of substrate‐induced ubiquitin transfer by UBR7‐PHD finger, a newly identified histone H2BK120 ubiquitin ligase
Monoubiquitination of histone H2B at lysine 120 plays a vital role in active transcription and
DNA damage response pathways. Ubiquitin protein ligase E3 component N‐recognin 7 …
DNA damage response pathways. Ubiquitin protein ligase E3 component N‐recognin 7 …
Insights into ubiquitination from the unique clamp-like binding of the RING E3 AO7 to the E2 UbcH5B
S Li, YH Liang, J Mariano, MB Metzger… - Journal of Biological …, 2015 - ASBMB
RING proteins constitute the largest class of E3 ubiquitin ligases. Unlike most RINGs, AO7
(RNF25) binds the E2 ubiquitin-conjugating enzyme, UbcH5B (UBE2D2), with strikingly high …
(RNF25) binds the E2 ubiquitin-conjugating enzyme, UbcH5B (UBE2D2), with strikingly high …
Structural basis for the RING-catalyzed synthesis of K63-linked ubiquitin chains
E Branigan, A Plechanovová, EG Jaffray… - Nature structural & …, 2015 - nature.com
RING E3 ligase–catalyzed formation of K63-linked ubiquitin chains by the Ube2V2–Ubc13
E2 complex is required in many important biological processes. Here we report the structure …
E2 complex is required in many important biological processes. Here we report the structure …
Structure of the yeast Bre1 RING domain
P Kumar, C Wolberger - Proteins: Structure, Function, and …, 2015 - Wiley Online Library
Monoubiquitination of histone H2B at Lys123 in yeast plays a critical role in regulating
transcription, mRNA export, DNA replication, and the DNA damage response. The RING E3 …
transcription, mRNA export, DNA replication, and the DNA damage response. The RING E3 …
Structural basis for role of ring finger protein RNF168 RING domain
Ubiquitin adducts surrounding DNA double-strand breaks (DSBs) have emerged as
molecular platforms important for the assembly of DNA damage mediator and repair …
molecular platforms important for the assembly of DNA damage mediator and repair …
The E3 ligase RNF8 regulates KU80 removal and NHEJ repair
L Feng, J Chen - Nature structural & molecular biology, 2012 - nature.com
The ubiquitination cascade has a key role in the assembly of repair and signaling proteins at
sites of double-strand DNA breaks. The E3 ubiquitin ligase RING finger protein 8 (RNF8) …
sites of double-strand DNA breaks. The E3 ubiquitin ligase RING finger protein 8 (RNF8) …
Activation of a primed RING E3-E2–ubiquitin complex by non-covalent ubiquitin
L Buetow, M Gabrielsen, NG Anthony, H Dou, A Patel… - Molecular cell, 2015 - cell.com
RING ubiquitin ligases (E3) recruit ubiquitin-conjugate enzymes (E2) charged with ubiquitin
(Ub) to catalyze ubiquitination. Non-covalent Ub binding to the backside of certain E2s …
(Ub) to catalyze ubiquitination. Non-covalent Ub binding to the backside of certain E2s …
Allosteric regulation of E2: E3 interactions promote a processive ubiquitination machine
RING finger proteins constitute the large majority of ubiquitin ligases (E3s) and function by
interacting with ubiquitin‐conjugating enzymes (E2s) charged with ubiquitin. How low …
interacting with ubiquitin‐conjugating enzymes (E2s) charged with ubiquitin. How low …
Molecular insights into the function of RING finger (RNF)-containing proteins hRNF8 and hRNF168 in Ubc13/Mms2-dependent ubiquitylation
SJ Campbell, RA Edwards, CCY Leung… - Journal of Biological …, 2012 - ASBMB
The repair of DNA double strand breaks by homologous recombination relies on the unique
topology of the chains formed by Lys-63 ubiquitylation of chromatin to recruit repair factors …
topology of the chains formed by Lys-63 ubiquitylation of chromatin to recruit repair factors …