IndraLab

Statements


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sparser
"Thus it seems likely that ASXL1 DEU also uses this ubiquitin interface to stabilize ubiquitin binding of BAP1 and stimulate activity."

sparser
"The cryo-EM map revealed BAP1 bound to the nucleosome in a catalytic conformation, with clearly resolved BAP1-nucleosome, ASXL1-nucleosome, BAP1-Ub, and ASXL1-Ub interfaces ( xref and fig."

sparser
"In this complex, BAP1 is the catalytic subunit and its activity is strongly dependent on the interaction with conserved DEUBiquitinase Adaptor (DEUBAD) domain of ASXLs that induces conformational changes able to increase BAP1 affinity for ubiquitin [ xref ]."

reach
"BAP1 Ub binding mutants, Y33A/I226A/F228A, L8A/F168A/N229A, and L35A/I214A/F228A/L230A were generated using gene synthesis (BioBasic) and then subcloned into a modified pENTR D-Topo plasmid (Life Technologies)."

sparser
"We have undertaken extensive mutational approaches to gain mechanistic insight into BAP1ubiquitin interaction."

sparser
"Our comparative thermodynamic analysis reveals that BAP1ubiquitin interaction is majorly driven by entropy factor which is unique amongst UCHs."

sparser
"Our study sheds light on BAP1 interaction with ubiquitin, which will be useful in understanding its enzymatic function."

sparser
"The cryo-EM map revealed BAP1 bound to the nucleosome in a catalytic conformation, with clearly resolved BAP1-nucleosome, ASXL1-nucleosome, BAP1-Ub, and ASXL1-Ub interfaces ( xref and xref )."

sparser
"However, mechanistic insights into BAP1ubiquitin interaction remain enigmatic."

sparser
"The thermodynamic analysis reveals that BAP1ubiquitin interaction is entropically driven."

sparser
"In the present work, we have shown how BAP1 interacts with the ubiquitin by studying the enzyme kinetics and thermodynamics of BAP1N–ubiquitin interaction."

sparser
"We have predicted a few residues in BAP1N that might play an important role in BAP1ubiquitin binding based on the ubiquitin-binding interface of analogous UCHs."

sparser
"The CTD of BAP1 interacts with monoubiquinated DEBAUD domain, which allosterically increases BAP1’s affinity for ubiquitin on H2A at Lys-119 H2A and stimulates deubiquitination [ xref , xref ]."

reach
"Thus, we hypothesized that Ub binding by the BAP1/DEUBAD complex without actual catalysis is important for DEUBAD monoubiquitination and we sought to investigate this possibility."