PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 18719126-0 2008 Dissecting the roles of MuB in Mu transposition: ATP regulation of DNA binding is not essential for target delivery. Adenosine Triphosphate 49-52 ubiquitin like 3 Homo sapiens 24-27 2965985-3 1988 Our results show that a differential distribution of Mu B protein between "immune" and "non-immune" DNA molecules is responsible for target immunity; in the presence of Mu A protein and ATP, Mu B protein dissociates preferentially from immune DNA molecules. Adenosine Triphosphate 186-189 ubiquitin like 3 Homo sapiens 53-57 2965985-3 1988 Our results show that a differential distribution of Mu B protein between "immune" and "non-immune" DNA molecules is responsible for target immunity; in the presence of Mu A protein and ATP, Mu B protein dissociates preferentially from immune DNA molecules. Adenosine Triphosphate 186-189 ubiquitin like 3 Homo sapiens 191-195 2965985-4 1988 Hydrolysis of ATP is implicated in establishing the differential distribution of Mu B protein between immune and non-immune DNA molecules in the presence of Mu A protein; nonhydrolyzable ATP gamma S can support an efficient strand-transfer reaction even with a target DNA that is immune in a reaction with ATP. Adenosine Triphosphate 14-17 ubiquitin like 3 Homo sapiens 81-85 2965985-4 1988 Hydrolysis of ATP is implicated in establishing the differential distribution of Mu B protein between immune and non-immune DNA molecules in the presence of Mu A protein; nonhydrolyzable ATP gamma S can support an efficient strand-transfer reaction even with a target DNA that is immune in a reaction with ATP. Adenosine Triphosphate 187-190 ubiquitin like 3 Homo sapiens 81-85 23776210-1 2013 MuB is an ATP-dependent nonspecific DNA-binding protein that regulates the activity of the MuA transposase and captures target DNA for transposition. Adenosine Triphosphate 10-13 ubiquitin like 3 Homo sapiens 0-3 23776210-4 2013 We demonstrate that MuB is an ATPase associated with diverse cellular activities (AAA+ ATPase) and forms ATP-dependent filaments with or without DNA. Adenosine Triphosphate 30-33 ubiquitin like 3 Homo sapiens 20-23 18719126-3 2008 Selection of appropriate target DNA requires ATP hydrolysis by the MuB ATPase. Adenosine Triphosphate 45-48 ubiquitin like 3 Homo sapiens 67-70 18719126-4 2008 By fusing MuB to a site-specific DNA-binding protein, the Arc repressor, we generated a MuB variant that could select target DNA independently of ATP. Adenosine Triphosphate 146-149 ubiquitin like 3 Homo sapiens 10-13 18719126-4 2008 By fusing MuB to a site-specific DNA-binding protein, the Arc repressor, we generated a MuB variant that could select target DNA independently of ATP. Adenosine Triphosphate 146-149 ubiquitin like 3 Homo sapiens 88-91 18719126-6 2008 We find that with the fusion proteins, MuB-dependent target delivery occurs efficiently under conditions where ATP hydrolysis is prevented by mutation or use of ADP. Adenosine Triphosphate 111-114 ubiquitin like 3 Homo sapiens 39-42 18719126-8 2008 These data indicate that the ATP- and MuA-regulated DNA-binding activity of MuB is not essential for target delivery but that activation of MuA by MuB strictly requires nucleotide-bound MuB. Adenosine Triphosphate 29-32 ubiquitin like 3 Homo sapiens 76-79 18719126-8 2008 These data indicate that the ATP- and MuA-regulated DNA-binding activity of MuB is not essential for target delivery but that activation of MuA by MuB strictly requires nucleotide-bound MuB. Adenosine Triphosphate 29-32 ubiquitin like 3 Homo sapiens 147-150 18719126-8 2008 These data indicate that the ATP- and MuA-regulated DNA-binding activity of MuB is not essential for target delivery but that activation of MuA by MuB strictly requires nucleotide-bound MuB. Adenosine Triphosphate 29-32 ubiquitin like 3 Homo sapiens 147-150 9736628-4 1998 We found that both MuB-ADP and MuB-ATP stimulate transposase, whereas only MuB-ATP binds with high affinity to DNA. Adenosine Triphosphate 35-38 ubiquitin like 3 Homo sapiens 31-34 12049743-4 2002 Additionally, ATP hydrolysis was obligatorily coupled to dissociation of MuB subunits from the DNA during polymer disassembly. Adenosine Triphosphate 14-17 ubiquitin like 3 Homo sapiens 73-76 9736628-4 1998 We found that both MuB-ADP and MuB-ATP stimulate transposase, whereas only MuB-ATP binds with high affinity to DNA. Adenosine Triphosphate 35-38 ubiquitin like 3 Homo sapiens 31-34 9736628-5 1998 Four different ATPase-defective MuB mutants fail to activate the normal transposition pathway, further indicating that ATP plays critical regulatory roles during transposition. Adenosine Triphosphate 15-18 ubiquitin like 3 Homo sapiens 32-35 9736628-7 1998 Based on these studies, we propose that the switch from the ATP- to ADP-bound form allows MuB to release the target DNA while maintaining its stimulatory interaction with transposase. Adenosine Triphosphate 60-63 ubiquitin like 3 Homo sapiens 90-93 9736628-8 1998 Thus, ATP-hydrolysis by MuB appears to function as a molecular switch controlling how target DNA is delivered to the core transposition machinery. Adenosine Triphosphate 6-9 ubiquitin like 3 Homo sapiens 24-27 9735286-6 1998 The defect in these proteins was also uniformly suppressed by either Mn2+, or the Mu B protein in the presence of ATP and target DNA. Adenosine Triphosphate 114-117 ubiquitin like 3 Homo sapiens 82-86 1654329-3 1991 We have previously shown that in the presence of ATP the Mu B protein can stimulate the Mu A-directed cleavage reaction of mini-Mu plasmids carrying a terminal base pair mutation (Surette, M.G., Harkness, T., and Chaconas, G. (1991) J. Biol. Adenosine Triphosphate 49-52 ubiquitin like 3 Homo sapiens 57-61 1654329-6 1991 Here we demonstrate that in the absence of a non-Mu DNA target molecule the Mu B protein stimulates intramolecular integration of a mini-Mu in an ATP-dependent fashion. Adenosine Triphosphate 146-149 ubiquitin like 3 Homo sapiens 76-80