PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 25620052-2 2015 Biosynthesis of all Hyd involves the insertion of a Fe(CN)2CO group and a subsequent insertion of nickel ions through the HypA/HybF, HypB and SlyD proteins. Nickel 98-104 hypA Escherichia coli 122-126 22384275-2 2012 Metal chaperone proteins HypA and HypB are required for the nickel insertion step of [NiFe]-hydrogenase maturation. Nickel 60-66 hypA Escherichia coli 25-29 23899293-2 2013 The two accessory proteins HypA and HypB interact with each other and are thought to cooperate to insert nickel into the active site of the hydrogenase-3 precursor protein. Nickel 105-111 hypA Escherichia coli 27-31 23899293-5 2013 This work lead to a re-evaluation of the HypA nickel affinity, revealing a KD on the order of 10(-8) M. HypA can efficiently remove nickel, but not zinc, from the metal-binding site in the GTPase domain of HypB, a process that is less efficient when complex formation between HypA and HypB is disrupted. Nickel 46-52 hypA Escherichia coli 41-45 23899293-5 2013 This work lead to a re-evaluation of the HypA nickel affinity, revealing a KD on the order of 10(-8) M. HypA can efficiently remove nickel, but not zinc, from the metal-binding site in the GTPase domain of HypB, a process that is less efficient when complex formation between HypA and HypB is disrupted. Nickel 46-52 hypA Escherichia coli 104-108 23899293-5 2013 This work lead to a re-evaluation of the HypA nickel affinity, revealing a KD on the order of 10(-8) M. HypA can efficiently remove nickel, but not zinc, from the metal-binding site in the GTPase domain of HypB, a process that is less efficient when complex formation between HypA and HypB is disrupted. Nickel 46-52 hypA Escherichia coli 104-108 23899293-5 2013 This work lead to a re-evaluation of the HypA nickel affinity, revealing a KD on the order of 10(-8) M. HypA can efficiently remove nickel, but not zinc, from the metal-binding site in the GTPase domain of HypB, a process that is less efficient when complex formation between HypA and HypB is disrupted. Nickel 132-138 hypA Escherichia coli 41-45 23899293-5 2013 This work lead to a re-evaluation of the HypA nickel affinity, revealing a KD on the order of 10(-8) M. HypA can efficiently remove nickel, but not zinc, from the metal-binding site in the GTPase domain of HypB, a process that is less efficient when complex formation between HypA and HypB is disrupted. Nickel 132-138 hypA Escherichia coli 104-108 23899293-5 2013 This work lead to a re-evaluation of the HypA nickel affinity, revealing a KD on the order of 10(-8) M. HypA can efficiently remove nickel, but not zinc, from the metal-binding site in the GTPase domain of HypB, a process that is less efficient when complex formation between HypA and HypB is disrupted. Nickel 132-138 hypA Escherichia coli 104-108 23899293-6 2013 Furthermore, nickel release from HypB to HypA is specifically accelerated when HypB is loaded with GDP, but not GTP. Nickel 13-19 hypA Escherichia coli 41-45 23899293-7 2013 These results are consistent with the HypA-HypB complex serving as a transfer step in the relay of nickel from membrane transporter to its final destination in the hydrogenase active site and suggest that this complex contributes to the metal fidelity of this pathway. Nickel 99-105 hypA Escherichia coli 38-42 22384275-3 2012 How HypA and HypB work together to deliver nickel to the catalytic core remains elusive. Nickel 43-49 hypA Escherichia coli 4-8 22384275-10 2012 The HypA binding site is in proximity to the metal binding site of HypB, suggesting that the HypA/HypB interaction may facilitate nickel transfer between the two proteins. Nickel 130-136 hypA Escherichia coli 4-8 22384275-10 2012 The HypA binding site is in proximity to the metal binding site of HypB, suggesting that the HypA/HypB interaction may facilitate nickel transfer between the two proteins. Nickel 130-136 hypA Escherichia coli 93-97 22016389-0 2011 Protein interactions and localization of the Escherichia coli accessory protein HypA during nickel insertion to [NiFe] hydrogenase. Nickel 92-98 hypA Escherichia coli 80-84 22016389-1 2011 Nickel delivery during maturation of Escherichia coli [NiFe] hydrogenase 3 includes the accessory proteins HypA, HypB, and SlyD. Nickel 0-6 hypA Escherichia coli 107-111 22016389-4 2011 Multiprotein complexes containing HypA, HypB, SlyD, and HycE were observed, consistent with the assembly of a single nickel insertion cluster. Nickel 117-123 hypA Escherichia coli 34-38 22016389-6 2011 The HypA-HycE complex was not detected in the absence of the HypC or HypD proteins, involved in the preceding iron insertion step, and this interaction is enhanced by nickel brought into the cell by the NikABCDE membrane transporter. Nickel 167-173 hypA Escherichia coli 4-8 22016389-8 2011 These results support the hypothesis that HypA acts as a scaffold for assembly of the nickel insertion proteins with the hydrogenase precursor protein after delivery of the iron center. Nickel 86-92 hypA Escherichia coli 42-46 22016389-9 2011 At different stages of the hydrogenase maturation process, HypA was observed at or near the cell membrane by using fluorescence confocal microscopy, as was HycE, suggesting membrane localization of the nickel insertion event. Nickel 202-208 hypA Escherichia coli 59-63 15090500-1 2004 HypA and HypB are maturation proteins required for incorporation of nickel into the hydrogenase large subunit. Nickel 68-74 hypA Escherichia coli 0-4 15995183-0 2005 Escherichia coli HypA is a zinc metalloprotein with a weak affinity for nickel. Nickel 72-78 hypA Escherichia coli 17-21 15995183-2 2005 HypA or a homologous protein is required for nickel insertion into the hydrogenase precursor proteins. Nickel 45-51 hypA Escherichia coli 0-4 15995183-8 2005 Fluorescence titration experiments demonstrate that HypA binds nickel with micromolar affinity and that the presence of zinc does not dramatically affect the nickel-binding activity. Nickel 63-69 hypA Escherichia coli 52-56 15995183-9 2005 Finally, complex formation between HypA and HypB, another accessory protein required for nickel insertion, was observed. Nickel 89-95 hypA Escherichia coli 35-39 15995183-10 2005 These experiments suggest that HypA is an architectural component of the hydrogenase metallocenter assembly pathway and that it may also have a direct role in the delivery of nickel to the hydrogenase large subunit. Nickel 175-181 hypA Escherichia coli 31-35 17464061-3 2007 Among the accessory/maturation proteins, the nickel-binding HypA protein has been previously shown to be required for the full activity of both the hydrogenase and the urease enzymes, while another nickel-binding protein, UreE, is known to be solely involved in the urease maturation process. Nickel 45-51 hypA Escherichia coli 60-64 17464061-3 2007 Among the accessory/maturation proteins, the nickel-binding HypA protein has been previously shown to be required for the full activity of both the hydrogenase and the urease enzymes, while another nickel-binding protein, UreE, is known to be solely involved in the urease maturation process. Nickel 198-204 hypA Escherichia coli 60-64 17464061-7 2007 By using a two-plasmid system in Escherichia coli, the highest urease activity was achieved under low nickel conditions only when the UreE protein was expressed along with the wild-type HypA protein, but not with its nickel-binding-deficient variant HypA H2A. Nickel 102-108 hypA Escherichia coli 186-190 17464061-9 2007 Although various attempts to show direct nickel transfer from HypA to UreE failed, these results suggest that interactions between the nickel-binding accessory proteins HypA and UreE are required to allow nickel transfer from HypA eventually to the apourease in H. pylori. Nickel 41-47 hypA Escherichia coli 62-66 17464061-9 2007 Although various attempts to show direct nickel transfer from HypA to UreE failed, these results suggest that interactions between the nickel-binding accessory proteins HypA and UreE are required to allow nickel transfer from HypA eventually to the apourease in H. pylori. Nickel 41-47 hypA Escherichia coli 169-173 17464061-9 2007 Although various attempts to show direct nickel transfer from HypA to UreE failed, these results suggest that interactions between the nickel-binding accessory proteins HypA and UreE are required to allow nickel transfer from HypA eventually to the apourease in H. pylori. Nickel 41-47 hypA Escherichia coli 169-173 17464061-9 2007 Although various attempts to show direct nickel transfer from HypA to UreE failed, these results suggest that interactions between the nickel-binding accessory proteins HypA and UreE are required to allow nickel transfer from HypA eventually to the apourease in H. pylori. Nickel 135-141 hypA Escherichia coli 62-66 17464061-9 2007 Although various attempts to show direct nickel transfer from HypA to UreE failed, these results suggest that interactions between the nickel-binding accessory proteins HypA and UreE are required to allow nickel transfer from HypA eventually to the apourease in H. pylori. Nickel 135-141 hypA Escherichia coli 169-173 17464061-9 2007 Although various attempts to show direct nickel transfer from HypA to UreE failed, these results suggest that interactions between the nickel-binding accessory proteins HypA and UreE are required to allow nickel transfer from HypA eventually to the apourease in H. pylori. Nickel 135-141 hypA Escherichia coli 169-173 17464061-9 2007 Although various attempts to show direct nickel transfer from HypA to UreE failed, these results suggest that interactions between the nickel-binding accessory proteins HypA and UreE are required to allow nickel transfer from HypA eventually to the apourease in H. pylori. Nickel 135-141 hypA Escherichia coli 62-66 17464061-9 2007 Although various attempts to show direct nickel transfer from HypA to UreE failed, these results suggest that interactions between the nickel-binding accessory proteins HypA and UreE are required to allow nickel transfer from HypA eventually to the apourease in H. pylori. Nickel 135-141 hypA Escherichia coli 169-173 17464061-9 2007 Although various attempts to show direct nickel transfer from HypA to UreE failed, these results suggest that interactions between the nickel-binding accessory proteins HypA and UreE are required to allow nickel transfer from HypA eventually to the apourease in H. pylori. Nickel 135-141 hypA Escherichia coli 169-173 15090500-10 2004 A triple mutant deficient in the synthesis or activity of HypA, HybF, and HypB was constructed, and it exhibited the same responsiveness for phenotypic complementation by high nickel as mutants with a single lesion in one of the genes exhibited. Nickel 176-182 hypA Escherichia coli 58-62 15090500-11 2004 The results are interpreted in terms of a concerted action of HypB and HybF in nickel insertion in which HybF (as well as its homolog, HypA) functions as a metallochaperone and HypB functions as a regulator that controls the interaction of HybF with the target protein. Nickel 79-85 hypA Escherichia coli 135-139 1482271-9 1992 It is concluded that the products of the hypA-E genes play a role in nickel incorporation into hydrogenase apoprotein and/or processing of the constituent subunits of this enzyme. Nickel 69-75 hypA Escherichia coli 41-45 12081959-11 2002 39:176-182, 2001) that HypA cooperates with HypB in the insertion of nickel into the precursor of the large hydrogenase subunit. Nickel 69-75 hypA Escherichia coli 23-27 31273981-0 2019 Bimodal Nickel-Binding Site on Escherichia coli [NiFe]-Hydrogenase Metallochaperone HypA. Nickel 8-14 hypA Escherichia coli 84-88 31273981-3 2019 The penultimate maturation step is the delivery of nickel to a primed hydrogenase enzyme precursor protein, a process that is accomplished by two nickel metallochaperones, the accessory protein HypA and the GTPase HypB. Nickel 51-57 hypA Escherichia coli 194-198 31273981-3 2019 The penultimate maturation step is the delivery of nickel to a primed hydrogenase enzyme precursor protein, a process that is accomplished by two nickel metallochaperones, the accessory protein HypA and the GTPase HypB. Nickel 146-152 hypA Escherichia coli 194-198 31273981-4 2019 Recent work demonstrated that nickel is rapidly transferred to HypA from GDP-loaded HypB within the context of a protein complex in a nickel selective and unidirectional process. Nickel 30-36 hypA Escherichia coli 63-67 31273981-4 2019 Recent work demonstrated that nickel is rapidly transferred to HypA from GDP-loaded HypB within the context of a protein complex in a nickel selective and unidirectional process. Nickel 134-140 hypA Escherichia coli 63-67 31273981-5 2019 To investigate the mechanism of metal transfer, we examined the allosteric effects of nucleotide cofactors and partner proteins on the nickel environments of HypA and HypB by using a combination of biochemical, microbiological, computational, and spectroscopic techniques. Nickel 135-141 hypA Escherichia coli 158-162 31273981-7 2019 In addition, interaction with a mutant version of HypA with disrupted nickel binding, H2Q-HypA, does not induce substantial changes to the HypB G-domain nickel site. Nickel 70-76 hypA Escherichia coli 50-54 31273981-7 2019 In addition, interaction with a mutant version of HypA with disrupted nickel binding, H2Q-HypA, does not induce substantial changes to the HypB G-domain nickel site. Nickel 70-76 hypA Escherichia coli 90-94 31273981-9 2019 Analysis of a peptide maquette derived from the N-terminus of HypA revealed that nickel is predominately coordinated by atoms from the N-terminal Met-His motif. Nickel 81-87 hypA Escherichia coli 62-66 31273981-10 2019 Furthermore, HypA is capable of two nickel-binding modes at the N-terminus, a HypB-induced mode and a binding mode that mirrors the peptide maquette. Nickel 36-42 hypA Escherichia coli 13-17 31273981-11 2019 Collectively, these results reveal that HypB brings about changes in the nickel coordination of HypA, providing a mechanism for the HypB-dependent control of the acquisition and release of nickel by HypA. Nickel 73-79 hypA Escherichia coli 96-100 31273981-11 2019 Collectively, these results reveal that HypB brings about changes in the nickel coordination of HypA, providing a mechanism for the HypB-dependent control of the acquisition and release of nickel by HypA. Nickel 73-79 hypA Escherichia coli 199-203 31273981-11 2019 Collectively, these results reveal that HypB brings about changes in the nickel coordination of HypA, providing a mechanism for the HypB-dependent control of the acquisition and release of nickel by HypA. Nickel 189-195 hypA Escherichia coli 96-100 31273981-11 2019 Collectively, these results reveal that HypB brings about changes in the nickel coordination of HypA, providing a mechanism for the HypB-dependent control of the acquisition and release of nickel by HypA. Nickel 189-195 hypA Escherichia coli 199-203 27951644-0 2016 Mechanism of Selective Nickel Transfer from HypB to HypA, Escherichia coli [NiFe]-Hydrogenase Accessory Proteins. Nickel 23-29 hypA Escherichia coli 52-56 31581740-3 2019 One of the most studied metallochaperones is the nickel-binding protein HypA, involved in the maturation of nickel-dependent hydrogenases and ureases. Nickel 49-55 hypA Escherichia coli 72-76 31581740-3 2019 One of the most studied metallochaperones is the nickel-binding protein HypA, involved in the maturation of nickel-dependent hydrogenases and ureases. Nickel 108-114 hypA Escherichia coli 72-76 30758762-2 2019 Nickel insertion during maturation of Escherichia coli [NiFe]-hydrogenase 3 is achieved by the metallochaperones HypA, SlyD and the GTPase HypB, but how these proteins cooperate to ensure nickel delivery is not known. Nickel 0-6 hypA Escherichia coli 113-117 27951644-2 2016 The synthesis of the bimetallic catalytic center requires a suite of accessory proteins, and the penultimate step, nickel insertion, is facilitated by the metallochaperones HypA and HypB. Nickel 115-121 hypA Escherichia coli 173-177 27951644-3 2016 In Escherichia coli, nickel moves from a site in the GTPase domain of HypB to HypA in a process accelerated by GDP. Nickel 21-27 hypA Escherichia coli 78-82 27951644-5 2016 Integral to this work was His2Gln HypA, a mutant with attenuated nickel affinity that does not support hydrogenase production in E. coli. Nickel 65-71 hypA Escherichia coli 34-38