PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 8253735-9 1993 Most importantly, the stimulation of ATP hydrolysis by high salt coincided with that of the induction of alpha-helix in RecA protein. Salts 60-64 RAD51 recombinase Homo sapiens 120-124 8420955-7 1993 At high salt condition, which induces ATPase activity in RecA just as DNA binding does, the tyrosine fluorescence is more pronounced than at low salt conditions, indicating that the effect induced by high salt is different from the conformational change induced by DNA binding. Salts 8-12 RAD51 recombinase Homo sapiens 57-61 8223609-8 1993 A protection of the histidine residues is also effected by high salt concentration which promotes, just as DNA binding, ATPase and coprotease activity in RecA. Salts 64-68 RAD51 recombinase Homo sapiens 154-158 8420955-7 1993 At high salt condition, which induces ATPase activity in RecA just as DNA binding does, the tyrosine fluorescence is more pronounced than at low salt conditions, indicating that the effect induced by high salt is different from the conformational change induced by DNA binding. Salts 145-149 RAD51 recombinase Homo sapiens 57-61 2148682-13 1990 These patterns are observed for recA-mediated ATP hydrolysis with either high salt concentrations or a poly(deoxythymidylic acid) [poly(dT)] cofactor, although the activation is observed at much lower ATP and ATP gamma S concentrations when poly(dT) is used. Salts 78-82 RAD51 recombinase Homo sapiens 32-36 2150915-0 1990 Activation of recA protein: the salt-induced structural transition. Salts 32-36 RAD51 recombinase Homo sapiens 14-18 2150915-1 1990 Purified recA protein is induced by high salt concentrations to hydrolyse ATP even in the absence of DNA. Salts 41-45 RAD51 recombinase Homo sapiens 9-13 2150915-4 1990 Indeed, the other enzymatic activity of recA, the proteolytic cleavage of the lexA repressor, is found to be inducible by the same salt concentrations as those of the structural transition. Salts 131-135 RAD51 recombinase Homo sapiens 40-44 3065521-5 1988 The addition of monovalent salt shifts the distribution of RecA protein between its various oligomeric states. Salts 27-31 RAD51 recombinase Homo sapiens 59-63 2909521-7 1989 For this reason, the variation of the DNA binding constant with the salt concentration is amplified, and the number of ion pairs formed between DNA and RecA obtained from the apparent salt dependence (11 ion pairs/monomer) has been overestimated. Salts 68-72 RAD51 recombinase Homo sapiens 152-156 2909521-7 1989 For this reason, the variation of the DNA binding constant with the salt concentration is amplified, and the number of ion pairs formed between DNA and RecA obtained from the apparent salt dependence (11 ion pairs/monomer) has been overestimated. Salts 184-188 RAD51 recombinase Homo sapiens 152-156 21857994-3 2011 Based on structural and functional homology with archaeal and yeast RAD51, we have identified the human RAD51 (HsRAD51) subunit interface residues HsRad51(F129) in the Walker A box and HsRad51(H294) in the L2 ssDNA binding region as potentially important participants in salt-induced conformational transitions essential for recombinase activity. Salts 271-275 RAD51 recombinase Homo sapiens 104-109 3981638-7 1985 In addition, the stability of the recA protein-DNA complex is very salt dependent (d log K/d log [NaC1] approximately -10) and it is the intrinsic binding affinity rather than the co-operativity of binding that is affected; thus, under all conditions observed, recA protein binds single-stranded DNA co-operatively with a value of omega = 50 +/- 10. Salts 67-71 RAD51 recombinase Homo sapiens 34-38 3981638-7 1985 In addition, the stability of the recA protein-DNA complex is very salt dependent (d log K/d log [NaC1] approximately -10) and it is the intrinsic binding affinity rather than the co-operativity of binding that is affected; thus, under all conditions observed, recA protein binds single-stranded DNA co-operatively with a value of omega = 50 +/- 10. Salts 67-71 RAD51 recombinase Homo sapiens 261-265 21857994-3 2011 Based on structural and functional homology with archaeal and yeast RAD51, we have identified the human RAD51 (HsRAD51) subunit interface residues HsRad51(F129) in the Walker A box and HsRad51(H294) in the L2 ssDNA binding region as potentially important participants in salt-induced conformational transitions essential for recombinase activity. Salts 271-275 RAD51 recombinase Homo sapiens 111-118 21857994-3 2011 Based on structural and functional homology with archaeal and yeast RAD51, we have identified the human RAD51 (HsRAD51) subunit interface residues HsRad51(F129) in the Walker A box and HsRad51(H294) in the L2 ssDNA binding region as potentially important participants in salt-induced conformational transitions essential for recombinase activity. Salts 271-275 RAD51 recombinase Homo sapiens 147-154 19133161-5 2009 Interestingly, salt at low concentration can substitute the role of RAD52, in facilitating aggregation of RAD51-dsDNA complexes, that concomitantly also leads to better unwinding. Salts 15-19 RAD51 recombinase Homo sapiens 106-111 19780587-2 2009 We observe that the electrophoretic force is 2-4 times larger for RecA-DNA filaments than for uncoated DNA molecules and that this force increases at lower salt concentrations. Salts 156-160 RAD51 recombinase Homo sapiens 66-70 19780587-5 2009 The conductance steps that occur when RecA-DNA enters the nanopore change from conductance decreases at high salt to conductance increases at low salt, which allows the apparent charge of the RecA-DNA filament to be extracted. Salts 109-113 RAD51 recombinase Homo sapiens 38-42 19780587-5 2009 The conductance steps that occur when RecA-DNA enters the nanopore change from conductance decreases at high salt to conductance increases at low salt, which allows the apparent charge of the RecA-DNA filament to be extracted. Salts 109-113 RAD51 recombinase Homo sapiens 192-196 19780587-5 2009 The conductance steps that occur when RecA-DNA enters the nanopore change from conductance decreases at high salt to conductance increases at low salt, which allows the apparent charge of the RecA-DNA filament to be extracted. Salts 146-150 RAD51 recombinase Homo sapiens 38-42 19780587-5 2009 The conductance steps that occur when RecA-DNA enters the nanopore change from conductance decreases at high salt to conductance increases at low salt, which allows the apparent charge of the RecA-DNA filament to be extracted. Salts 146-150 RAD51 recombinase Homo sapiens 192-196 16780572-4 2006 Gel retardation and DNA-dependent ATP hydrolysis measurements revealed that the substitution of the tyrosine residue at position 232 (Tyr232) within the L1 loop with alanine, a short side chain amino acid, significantly decreased the DNA-binding ability of human Rad51, without affecting the protein folding or the salt-induced, DNA-independent ATP hydrolysis. Salts 315-319 RAD51 recombinase Homo sapiens 263-268 18196977-5 2008 Thermodynamic measurements of the equilibrium-binding properties of these complexes showed that (dT)(24) promoted a more salt sensitive complex than the one formed with (dT)(16), indicating more ionic interactions between RecA and DNA in the former. Salts 121-125 RAD51 recombinase Homo sapiens 222-226 16909421-6 2006 Predictions of the model are in agreement with Small Angle Neutron Scattering (SANS) measurements of the filament helix pitch in RecA::ADP-AlF(4) complex at various salt concentrations. Salts 165-169 RAD51 recombinase Homo sapiens 129-133 11061970-4 2000 Finally, we show that the role of DNA and high salt in the stimulation of the ATPase of RecA is to stabilize this highly mobile region involved in hydrolysis. Salts 47-51 RAD51 recombinase Homo sapiens 88-92 16644292-18 2006 These salt-induced characteristics of hRAD51 increasingly resemble RecA-mediated recombinase activities, which should help in dissecting the mechanism of these proteins in homologous recombination. Salts 6-10 RAD51 recombinase Homo sapiens 38-44 16644292-18 2006 These salt-induced characteristics of hRAD51 increasingly resemble RecA-mediated recombinase activities, which should help in dissecting the mechanism of these proteins in homologous recombination. Salts 6-10 RAD51 recombinase Homo sapiens 67-71 16644292-1 2006 Previous work by Sung and colleagues identified unusual salt requirements for hRAD51 strand exchange compared to RecA [S. Sigurdsson, K. Trujillo, B. Salts 56-60 RAD51 recombinase Homo sapiens 78-84 16644292-5 2006 Later studies showed that this salt [(NH4)2SO4] appeared to enhance the ability of hRAD51 to distinguish ssDNA from dsDNA [Y. Liu, A.Z. Salts 31-35 RAD51 recombinase Homo sapiens 83-89 15033353-9 2004 Most importantly, high salt induces a conformational change in RAD51, leading to the formation of extended nucleoprotein filaments on ssDNA. Salts 23-27 RAD51 recombinase Homo sapiens 63-68 12801910-0 2003 pH- and salt-dependent self-assembly of human Rad51 protein analyzed as fluorescence resonance energy transfer between labeled proteins. Salts 8-12 RAD51 recombinase Homo sapiens 46-51 9325305-4 1997 High salt activation of RecA function is also disrupted by these mutations. Salts 5-9 RAD51 recombinase Homo sapiens 24-28