PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
23283730-6	2013	Binding of single-stranded oligonucleotides [one molecule of (dT)(70), one molecule of (dT)(35), or two molecules of (dT)(35)] was found to prevent SSB subunit exchange.	Thymidine	62-64	single-stranded DNA-binding protein	Escherichia coli	148-151	
23283730-6	2013	Binding of single-stranded oligonucleotides [one molecule of (dT)(70), one molecule of (dT)(35), or two molecules of (dT)(35)] was found to prevent SSB subunit exchange.	Thymidine	88-90	single-stranded DNA-binding protein	Escherichia coli	148-151	
23283730-6	2013	Binding of single-stranded oligonucleotides [one molecule of (dT)(70), one molecule of (dT)(35), or two molecules of (dT)(35)] was found to prevent SSB subunit exchange.	Thymidine	88-90	single-stranded DNA-binding protein	Escherichia coli	148-151	
16618108-2	2006	Using isothermal titration calorimetry we have now examined DeltaH(obs) over a much wider temperature range (5-60 degrees C) and as a function of monovalent salt concentration and type for SSB binding to (dT)(70) under solution conditions that favor the fully wrapped (SSB)(65) complex (monovalent salt concentration >or=0.20 M).	Thymidine	205-207	single-stranded DNA-binding protein	Escherichia coli	189-192	
22543099-5	2012	We also present a crystal structure at 2.1 A resolution of the Pf-SSB tetramer bound to two (dT)(35) molecules.	Thymidine	93-95	single-stranded DNA-binding protein	Escherichia coli	66-69	
21636209-0	2011	E. coli SSB tetramer binds the first and second molecules of (dT)(35) with heat capacities of opposite sign.	Thymidine	62-64	single-stranded DNA-binding protein	Escherichia coli	8-11	
21636209-1	2011	We have previously shown that formation of a 1:1 fully wrapped complex of Escherichia coli SSB tetramer with (dT)(70) displays a temperature-dependent sign reversal of the binding heat capacity (DeltaC(P)).	Thymidine	110-112	single-stranded DNA-binding protein	Escherichia coli	91-94	
17490681-2	2007	Here, we present direct evidence for fluctuations between the two major modes of SSB binding, (SSB)(35) and (SSB)(65) formed on (dT)(70), with rates of interconversion on time scales that vary as much as 200-fold for a mere fourfold change in NaCl concentration.	Thymidine	129-131	single-stranded DNA-binding protein	Escherichia coli	81-84	
17490681-2	2007	Here, we present direct evidence for fluctuations between the two major modes of SSB binding, (SSB)(35) and (SSB)(65) formed on (dT)(70), with rates of interconversion on time scales that vary as much as 200-fold for a mere fourfold change in NaCl concentration.	Thymidine	129-131	single-stranded DNA-binding protein	Escherichia coli	95-98	
17490681-2	2007	Here, we present direct evidence for fluctuations between the two major modes of SSB binding, (SSB)(35) and (SSB)(65) formed on (dT)(70), with rates of interconversion on time scales that vary as much as 200-fold for a mere fourfold change in NaCl concentration.	Thymidine	129-131	single-stranded DNA-binding protein	Escherichia coli	95-98	
16618108-2	2006	Using isothermal titration calorimetry we have now examined DeltaH(obs) over a much wider temperature range (5-60 degrees C) and as a function of monovalent salt concentration and type for SSB binding to (dT)(70) under solution conditions that favor the fully wrapped (SSB)(65) complex (monovalent salt concentration >or=0.20 M).	Thymidine	205-207	single-stranded DNA-binding protein	Escherichia coli	269-272	
10353851-2	1999	We have determined DeltaH1,obs for the binding of 1 mole of each of dT(pT)34, dC(pC)34, and dA(pA)34 to the SSB tetramer (20 mM NaCl at pH 8.1).	Thymidine	68-70	single-stranded DNA-binding protein	Escherichia coli	108-111	
16298996-1	2006	The effect of Mg2+ on the binding of the Streptococcus pneumoniae single-stranded DNA binding (SSB) proteins, SsbA and SsbB, to various dT(n) oligomers was examined by polyacrylamide gel electrophoresis.	Thymidine	136-138	single-stranded DNA-binding protein	Escherichia coli	95-98	
16298996-3	2006	In the absence of Mg2+, the results indicated that the SsbEc protein was able to bind to the dT(n) oligomers in the SSB(35) mode, with only two of the four subunits of the tetramer interacting with the dT(n) oligomers.	Thymidine	93-95	single-stranded DNA-binding protein	Escherichia coli	116-119	
11993998-2	2002	Under these conditions, a so-called (SSB)(65) complex is formed in which either one molecule of (dT)(70) or two molecules of (dT)(35) bind per tetramer.	Thymidine	97-99	single-stranded DNA-binding protein	Escherichia coli	37-40	
11993998-2	2002	Under these conditions, a so-called (SSB)(65) complex is formed in which either one molecule of (dT)(70) or two molecules of (dT)(35) bind per tetramer.	Thymidine	126-128	single-stranded DNA-binding protein	Escherichia coli	37-40	
11013397-4	2000	In an attempt to determine the origins of this heat capacity change, we have examined by isothermal titration calorimetry (ITC) the equilibrium binding of dT(pT)(34) to SSB over a broad pH range (pH 5.	Thymidine	155-157	single-stranded DNA-binding protein	Escherichia coli	169-172	
11013397-6	2000	A net protonation of the SSB protein occurs upon dT(pT)(34) binding over this entire pH range, with contributions from at least three sets of protonation sites (pK(a1) = 5.9-6.6, pK(a2) = 8.2-8.4, and pK(a3) = 10.2-10.3) and these protonation equilibria contribute substantially to the observed DeltaH and DeltaC(p) for the SSB-dT(pT)(34) interaction.	Thymidine	49-51	single-stranded DNA-binding protein	Escherichia coli	25-28	
9515699-6	1998	In searching for particular characteristics of RecA(Pa) in comparison with RecA(Ec), RecA441 and RecA803 proteins, RecA(Pa) showed unusually high abilities: to be resistant to the displacement by SSB protein from poly(dT); to stabilize a ternary complex RecA::ATP::ssDNA to high salt concentrations; and to be much more rapid in both the nucleation of double-stranded DNA (dsDNA) and the steady-state rate of dsDNA-dependent ATP hydrolysis at pH7.5.	Thymidine	218-220	single-stranded DNA-binding protein	Escherichia coli	196-199	
9600857-9	1998	Under conditions where we can determine DeltaG degrees obs, DeltaS degrees obs, and DeltaHobs (25 degrees C, pH 8.1, 0.17 to 2 M NaBr), SSB binding to dT(pT)69 is enthalpically driven with a large unfavorable entropic contribution, both of which are dependent upon [NaBr].	Thymidine	151-153	single-stranded DNA-binding protein	Escherichia coli	136-139	
9127948-8	1997	The increased intra-tetramer negative cooperativity makes it more difficult for ss-DNA to bind the third and fourth subunits of the W54S tetramer, explaining the increased stability of the (SSB)35 mode in complexes with poly(dT).	Thymidine	225-227	single-stranded DNA-binding protein	Escherichia coli	190-193	
8611514-5	1996	We also measured delta Hobs and its dependence on [NaCl] for SSB binding dT(pT)69 by ITC and find delta Hobs = -144 +/- 4 kcal/mol (0.175 M NaCl, pH 8.1, 25 degrees C) and [symbol see text] delta Hobs/ [symbol see text] log [NaCl] = 46 +/- 2 kcal/ mol (0.175-2.0 M NaCl).	Thymidine	73-75	single-stranded DNA-binding protein	Escherichia coli	61-64	
7947696-10	1994	The binding of SSB to dT(pT)n and dC(pC)n occurs with delta H0 < 0 and delta C0P,obs = 0, since the bases in these ss-DNA molecules do not stack appreciably.	Thymidine	22-24	single-stranded DNA-binding protein	Escherichia coli	15-18	
8193130-1	1994	We have examined the ability of the Escherichia coli single-stranded DNA binding protein (SSB) tetramer to form its different binding modes on poly(dC), poly(U), and poly(A) over a range of NaCl and NaF concentrations for comparison with previous studies with poly(dT).	Thymidine	265-267	single-stranded DNA-binding protein	Escherichia coli	90-93	
1627560-6	1992	We have examined the effects of multivalent cations, principally the polyamine spermine, on the SSB-ss poly(dT) binding mode transitions and find that the transition from the (SSB)35 to the (SSB)56 binding mode can be induced by micromolar concentrations of polyamines as well as the inorganic cation Co(NH3)6(3+).	Thymidine	107-111	single-stranded DNA-binding protein	Escherichia coli	96-99	
1627560-7	1992	Furthermore, these multivalent cations, as well as Mg2+, induce the binding mode transition by binding cooperatively to the SSB-poly(dT) complexes.	Thymidine	133-135	single-stranded DNA-binding protein	Escherichia coli	124-127	
1988680-7	1991	At lower SSB-1 concentrations, SSB-1 monomers bind dT(pT)15 without negative co-operativity; however, the intrinsic affinity of dT(pT)15 for the monomer is a factor of approximately 10 lower than for the protomer (50 mM-NaCl, pH 8.1, 25 degrees C).	Thymidine	51-53	single-stranded DNA-binding protein	Escherichia coli	31-34	
3289611-4	1988	However, when the NaCl concentration is lowered, the overall affinity of dT(pT)34 for the second site on the SSB tetramer decreases dramatically.	Thymidine	73-75	single-stranded DNA-binding protein	Escherichia coli	109-112	
2661832-6	1989	The stoichiometries for saturation of the SSB tetramer are 4, 2, 2, 1 and 1, for the oligonucleotides, dT(pT)N-1, with N = 16, 28, 35, 56 and 70, respectively, indicating that one molecule of either dT(pT)27 or dT(pT)34 interacts with two SSB subunits, whereas one molecule of dT(pT)15 interacts with only a single subunit.	Thymidine	103-105	single-stranded DNA-binding protein	Escherichia coli	42-45	
2661832-6	1989	The stoichiometries for saturation of the SSB tetramer are 4, 2, 2, 1 and 1, for the oligonucleotides, dT(pT)N-1, with N = 16, 28, 35, 56 and 70, respectively, indicating that one molecule of either dT(pT)27 or dT(pT)34 interacts with two SSB subunits, whereas one molecule of dT(pT)15 interacts with only a single subunit.	Thymidine	199-201	single-stranded DNA-binding protein	Escherichia coli	42-45	
2661832-6	1989	The stoichiometries for saturation of the SSB tetramer are 4, 2, 2, 1 and 1, for the oligonucleotides, dT(pT)N-1, with N = 16, 28, 35, 56 and 70, respectively, indicating that one molecule of either dT(pT)27 or dT(pT)34 interacts with two SSB subunits, whereas one molecule of dT(pT)15 interacts with only a single subunit.	Thymidine	199-201	single-stranded DNA-binding protein	Escherichia coli	42-45	
2661832-6	1989	The stoichiometries for saturation of the SSB tetramer are 4, 2, 2, 1 and 1, for the oligonucleotides, dT(pT)N-1, with N = 16, 28, 35, 56 and 70, respectively, indicating that one molecule of either dT(pT)27 or dT(pT)34 interacts with two SSB subunits, whereas one molecule of dT(pT)15 interacts with only a single subunit.	Thymidine	199-201	single-stranded DNA-binding protein	Escherichia coli	42-45	
2661832-7	1989	Saturation of the SSB tetramer with dT(pT)15, dT(pT)34, dT(pT)69 or poly(dT) results in 85 to 90% quenching of the SSB fluorescence, whereas saturation with dT(pT)27 or dT(pT)55 results in only 80% and 72% quenching, respectively.	Thymidine	36-38	single-stranded DNA-binding protein	Escherichia coli	18-21	
2661832-7	1989	Saturation of the SSB tetramer with dT(pT)15, dT(pT)34, dT(pT)69 or poly(dT) results in 85 to 90% quenching of the SSB fluorescence, whereas saturation with dT(pT)27 or dT(pT)55 results in only 80% and 72% quenching, respectively.	Thymidine	36-38	single-stranded DNA-binding protein	Escherichia coli	115-118	
2661832-7	1989	Saturation of the SSB tetramer with dT(pT)15, dT(pT)34, dT(pT)69 or poly(dT) results in 85 to 90% quenching of the SSB fluorescence, whereas saturation with dT(pT)27 or dT(pT)55 results in only 80% and 72% quenching, respectively.	Thymidine	46-48	single-stranded DNA-binding protein	Escherichia coli	18-21	
2661832-7	1989	Saturation of the SSB tetramer with dT(pT)15, dT(pT)34, dT(pT)69 or poly(dT) results in 85 to 90% quenching of the SSB fluorescence, whereas saturation with dT(pT)27 or dT(pT)55 results in only 80% and 72% quenching, respectively.	Thymidine	46-48	single-stranded DNA-binding protein	Escherichia coli	115-118	
2661832-7	1989	Saturation of the SSB tetramer with dT(pT)15, dT(pT)34, dT(pT)69 or poly(dT) results in 85 to 90% quenching of the SSB fluorescence, whereas saturation with dT(pT)27 or dT(pT)55 results in only 80% and 72% quenching, respectively.	Thymidine	46-48	single-stranded DNA-binding protein	Escherichia coli	18-21	
2661832-7	1989	Saturation of the SSB tetramer with dT(pT)15, dT(pT)34, dT(pT)69 or poly(dT) results in 85 to 90% quenching of the SSB fluorescence, whereas saturation with dT(pT)27 or dT(pT)55 results in only 80% and 72% quenching, respectively.	Thymidine	46-48	single-stranded DNA-binding protein	Escherichia coli	115-118	
2661832-7	1989	Saturation of the SSB tetramer with dT(pT)15, dT(pT)34, dT(pT)69 or poly(dT) results in 85 to 90% quenching of the SSB fluorescence, whereas saturation with dT(pT)27 or dT(pT)55 results in only 80% and 72% quenching, respectively.	Thymidine	46-48	single-stranded DNA-binding protein	Escherichia coli	18-21	
2661832-7	1989	Saturation of the SSB tetramer with dT(pT)15, dT(pT)34, dT(pT)69 or poly(dT) results in 85 to 90% quenching of the SSB fluorescence, whereas saturation with dT(pT)27 or dT(pT)55 results in only 80% and 72% quenching, respectively.	Thymidine	46-48	single-stranded DNA-binding protein	Escherichia coli	115-118	
2661832-7	1989	Saturation of the SSB tetramer with dT(pT)15, dT(pT)34, dT(pT)69 or poly(dT) results in 85 to 90% quenching of the SSB fluorescence, whereas saturation with dT(pT)27 or dT(pT)55 results in only 80% and 72% quenching, respectively.	Thymidine	46-48	single-stranded DNA-binding protein	Escherichia coli	18-21	
2661832-7	1989	Saturation of the SSB tetramer with dT(pT)15, dT(pT)34, dT(pT)69 or poly(dT) results in 85 to 90% quenching of the SSB fluorescence, whereas saturation with dT(pT)27 or dT(pT)55 results in only 80% and 72% quenching, respectively.	Thymidine	46-48	single-stranded DNA-binding protein	Escherichia coli	115-118	
2661832-7	1989	Saturation of the SSB tetramer with dT(pT)15, dT(pT)34, dT(pT)69 or poly(dT) results in 85 to 90% quenching of the SSB fluorescence, whereas saturation with dT(pT)27 or dT(pT)55 results in only 80% and 72% quenching, respectively.	Thymidine	46-48	single-stranded DNA-binding protein	Escherichia coli	18-21	
2661832-7	1989	Saturation of the SSB tetramer with dT(pT)15, dT(pT)34, dT(pT)69 or poly(dT) results in 85 to 90% quenching of the SSB fluorescence, whereas saturation with dT(pT)27 or dT(pT)55 results in only 80% and 72% quenching, respectively.	Thymidine	46-48	single-stranded DNA-binding protein	Escherichia coli	115-118	
2661832-9	1989	A quenching of 50(+/- 2)% is observed upon filling only half of the subunits with either one molecule of dT(pT)34 or two molecules of dT(pT)15, which agrees with the quenching and site size observed in the (SSB)35 polynucleotide binding mode.	Thymidine	105-107	single-stranded DNA-binding protein	Escherichia coli	207-210	
2645140-0	1989	Modulation of the affinity of the single-stranded DNA-binding protein of Escherichia coli (E. coli SSB) to poly(dT) by site-directed mutagenesis.	Thymidine	112-114	single-stranded DNA-binding protein	Escherichia coli	99-102	
3060358-14	1988	These results are confirmed further by specific effects observed on the ODMR signals of pIP231a SSB upon binding to poly(Br5U) and poly(dT), which are known to be caused by the stacking of Trp54 with nucleic acid bases.	Thymidine	136-138	single-stranded DNA-binding protein	Escherichia coli	96-99	
3289611-1	1988	We have examined the binding of the oligonucleotide dT (pT)34 to the Escherichia coli SSB protein as a function of NaCl and MgCl2 concentration (25 degrees C, pH 8.1) by monitoring the quenching of the intrinsic protein fluorescence.	Thymidine	52-54	single-stranded DNA-binding protein	Escherichia coli	86-89	
3289611-2	1988	We find two binding sites for dT(pT)34 per single strand binding (SSB) protein tetramer, with each site possessing widely different affinities depending on the salt concentration.	Thymidine	30-32	single-stranded DNA-binding protein	Escherichia coli	66-69	
3280566-6	1988	"Reverse" titrations that monitor the quenching of the intrinsic tryptophan fluorescence of the SSB protein upon addition of poly(dT) have been used to measure the apparent site size of the complex at 25 degrees C in pH 8.1 and 6.9 as a function of NaF, NaCl, NaBr, and MgCl2 concentrations.	Thymidine	130-133	single-stranded DNA-binding protein	Escherichia coli	96-99	
2184887-1	1990	The time course of the reaction of Escherichia coli single-stranded DNA binding protein (E. coli SSB) with poly(dT) and M13mp8 single-stranded DNA has been measured by fluorescence stopped-flow experiments.	Thymidine	112-114	single-stranded DNA-binding protein	Escherichia coli	52-87	
2184887-1	1990	The time course of the reaction of Escherichia coli single-stranded DNA binding protein (E. coli SSB) with poly(dT) and M13mp8 single-stranded DNA has been measured by fluorescence stopped-flow experiments.	Thymidine	112-114	single-stranded DNA-binding protein	Escherichia coli	97-100	
2184887-2	1990	For poly(dT), the fluorescence traces follow simple bimolecular behavior up to 80% saturation of the polymer with E. coli SSB.	Thymidine	9-11	single-stranded DNA-binding protein	Escherichia coli	122-125	
7925378-5	1994	The association-rate constant for binding to poly(dT) is 3.2 x 10(8) M-1 s-1 for P. mirabilis SSB (PmiSSB) and 3.4 x 10(8) M-1 s-1 for S. marcescens SSB (SmaSSB).	Thymidine	50-53	single-stranded DNA-binding protein	Escherichia coli	94-97	
7925378-5	1994	The association-rate constant for binding to poly(dT) is 3.2 x 10(8) M-1 s-1 for P. mirabilis SSB (PmiSSB) and 3.4 x 10(8) M-1 s-1 for S. marcescens SSB (SmaSSB).	Thymidine	50-53	single-stranded DNA-binding protein	Escherichia coli	102-105	
3289611-5	1988	At 1.5 mM NaCl, only a single molecule of dT(pT)34 can bind per SSB tetramer, even with a 10-fold molar excess of dT(pT)34.	Thymidine	42-44	single-stranded DNA-binding protein	Escherichia coli	64-67	
3300806-0	1987	Complexes of the single-stranded DNA-binding protein from Escherichia coli (Eco SSB) with poly(dT).	Thymidine	95-97	single-stranded DNA-binding protein	Escherichia coli	80-83	
3322418-5	1987	Spin-orbit coupling between radiative singlet states and the Tx sublevel of the lowest triplet state of Trp 54 is enhanced selectively upon complexing of Eco SSB with poly(dT).	Thymidine	172-174	single-stranded DNA-binding protein	Escherichia coli	158-161	
3280021-16	1988	The SSB-poly(dT) affinity is too high to measure in buffers containing even 5 M NaCl; however, in 1.8-2.5 M NaBr, we measure alpha log Kobsd/alpha log [NaBr] = -5.7 +/- 0.7, with a lower value of omega T/O = 130 +/- 70.	Thymidine	13-15	single-stranded DNA-binding protein	Escherichia coli	4-7	
6298232-3	1983	Since poly(dT), but not d(pT)16, increases the rate of this reaction, it appears that cooperative SSB binding to single-stranded DNA (ssDNA) is associated with a conformational change that increases the exposure of the COOH terminus to proteolysis.	Thymidine	11-13	single-stranded DNA-binding protein	Escherichia coli	98-101	
2953903-4	1987	Also, when SSB protein is added after the formation of a RecA protein-single-stranded DNA complex using either etheno M13 DNA, poly(dA) or poly(dT), or using single-stranded phage M13 DNA at lower temperature (25 degrees C) and magnesium chloride concentrations of 1 mM or 4 mM, a time-dependent inhibition of activity is observed.	Thymidine	144-146	single-stranded DNA-binding protein	Escherichia coli	11-14	
3542037-1	1986	Four distinct binding modes for the interaction of Escherichia coli single-strand binding (SSB) protein with single-stranded (ss) DNA have been identified on the basis of quantitative titrations that monitor the quenching of the SSB protein fluorescence upon binding to the homopolynucleotide poly(dT) over a range of MgCl2 and NaCl concentrations at 25 and 37 degrees C. This is the first observation of multiple binding modes for a single protein binding to DNA.	Thymidine	298-300	single-stranded DNA-binding protein	Escherichia coli	91-94	
3542037-1	1986	Four distinct binding modes for the interaction of Escherichia coli single-strand binding (SSB) protein with single-stranded (ss) DNA have been identified on the basis of quantitative titrations that monitor the quenching of the SSB protein fluorescence upon binding to the homopolynucleotide poly(dT) over a range of MgCl2 and NaCl concentrations at 25 and 37 degrees C. This is the first observation of multiple binding modes for a single protein binding to DNA.	Thymidine	298-300	single-stranded DNA-binding protein	Escherichia coli	229-232	
7028102-10	1981	In the cooperative complexes with poly(dT) or poly(dA), all four binding sites on the ssB tetramer are also occupied.	Thymidine	39-42	single-stranded DNA-binding protein	Escherichia coli	86-89