Functional roles of conserved amino acid residues surrounding the phosphorylatable histidine of the yeast phosphorelay protein YPD1

Janiak‐Spens, Fabiola; West, Ann H.

doi:10.1046/j.1365-2958.2000.01973.x

Cited by 40 publications

(54 citation statements)

References 28 publications

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“…Surprisingly, however, mutagenesis of the corresponding residues in Ypd1 (K67A and Q86A) seems to have little effect on the ability to transfer phosphoryl groups to and from response regulator proteins (40). Similar results have been obtained with the corresponding Gln3 Ala mutation in ArcB C (41).…”

Section: Mutations Of Conserved Hpt Residues Block the Atp-dependent supporting

confidence: 67%

Crystal Structure of the CheA Histidine Phosphotransfer Domain that Mediates Response Regulator Phosphorylation in Bacterial Chemotaxis

Mourey¹,

Re²,

Pédelacq³

et al. 2001

Journal of Biological Chemistry

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The x-ray crystal structure of the P1 or H domain of the Salmonella CheA protein has been solved at 2.1-Å resolution. The structure is composed of an up-down up-down four-helix bundle that is typical of histidine phosphotransfer or HPt domains such as Escherichia coli ArcB C and Saccharomyces cerevisiae Ypd1. Loop regions and additional structural features distinguish all three proteins. The CheA domain has an additional Cterminal helix that lies over the surface formed by the C and D helices. The phosphoaccepting His-48 is located at a solvent-exposed position in the middle of the B helix where it is surrounded by several residues that are characteristic of other HPt domains. Mutagenesis studies indicate that conserved glutamate and lysine residues that are part of a hydrogen-bond network with His-48 are essential for the ATP-dependent phosphorylation reaction but not for the phosphotransfer reaction with CheY. These results suggest that the CheA-P1 domain may serve as a good model for understanding the general function of HPt domains in complex two-component phosphorelay systems.The signal transduction system that controls motor behavior in Salmonella and Escherichia coli provides a paradigm for understanding the biochemistry of intracellular information processing networks (for recent reviews see Refs.

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Section: Mutations Of Conserved Hpt Residues Block the Atp-dependent supporting

confidence: 67%

Crystal Structure of the CheA Histidine Phosphotransfer Domain that Mediates Response Regulator Phosphorylation in Bacterial Chemotaxis

Mourey¹,

Re²,

Pédelacq³

et al. 2001

Journal of Biological Chemistry

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“…Subsequently, the phosphate group is transferred to His64 on Ypd1p and further to Asp554 on Ssk1p. This sequence of events has been demonstrated convincingly by analysis of truncated and mutated proteins both in vivo and in vitro (256)(257)(258)476). These studies also demonstrate that in vivo the histidine kinase cannot bypass the Sln1p response regulator.…”

Section: Hog Map Kinase Pathway In S Cerevisiaementioning

confidence: 64%

“…Transfer from Sln1p His576 to Asp1144 was reported to be unidirectional, while that from Sln1p Asp1144 to Ypd1p His64 was reversible. The entire reaction is, however, driven towards phosphorylation of Ssk1p, since the equilibrium of the reaction from Ypd1p His64 to Ssk1p Asp554 was on the side of the latter (256)(257)(258). It was observed that Ypd1p has a significant stabilizing effect on phospho-Ssk1p; this effect is much less pronounced with a mutant version of Ypd1p that cannot be phosphorylated (256).…”

Section: Hog Map Kinase Pathway In S Cerevisiaementioning

confidence: 99%

Osmotic Stress Signaling and Osmoadaptation in Yeasts

Hohmann

2002

Microbiol Mol Biol Rev

1,515

1,440

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The ability to adapt to altered availability of free water is a fundamental property of living cells. The principles underlying osmoadaptation are well conserved. The yeast Saccharomyces cerevisiae is an excellent model system with which to study the molecular biology and physiology of osmoadaptation. Upon a shift to high osmolarity, yeast cells rapidly stimulate a mitogen-activated protein (MAP) kinase cascade, the high-osmolarity glycerol (HOG) pathway, which orchestrates part of the transcriptional response. The dynamic operation of the HOG pathway has been well studied, and similar osmosensing pathways exist in other eukaryotes. Protein kinase A, which seems to mediate a response to diverse stress conditions, is also involved in the transcriptional response program. Expression changes after a shift to high osmolarity aim at adjusting metabolism and the production of cellular protectants. Accumulation of the osmolyte glycerol, which is also controlled by altering transmembrane glycerol transport, is of central importance. Upon a shift from high to low osmolarity, yeast cells stimulate a different MAP kinase cascade, the cell integrity pathway. The transcriptional program upon hypo-osmotic shock seems to aim at adjusting cell surface properties. Rapid export of glycerol is an important event in adaptation to low osmolarity. Osmoadaptation, adjustment of cell surface properties, and the control of cell morphogenesis, growth, and proliferation are highly coordinated processes. The Skn7p response regulator may be involved in coordinating these events. An integrated understanding of osmoadaptation requires not only knowledge of the function of many uncharacterized genes but also further insight into the time line of events, their interdependence, their dynamics, and their spatial organization as well as the importance of subtle effects

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“…Comparison of residues predicted to be at the Hpt/ ChpArec interface based on the Rhodobacter sphaeroides CheA2 Hpt-CheY6 complex crystal structure Protein Data Bank code 3KYJ (41) reveals that Hpt1 does not share any of the four predicted interface residues located on the ␣A helix of Hpt2-6, including a conserved Phe, and only three out of the six residues on the ␣B helix (data not shown), consistent with the possibility that Hpt1 has diminished affinity for ChpArec. Additionally, the Lys at position H ϩ 3 that is found in Hpt2-6 and is missing from Hpt1 is required for efficient phosphorylation of the YPD1 Hpt protein by partner and non-partner receiver domains (42). Similarly, the absence in Hpt1 of an Arg at position H Ϫ 3 that is present in Hpt2-6 may contribute to the diminished reactivity of Hpt1 (32).…”

Section: Discussionmentioning

confidence: 99%

Phosphoryl Group Flow within the Pseudomonas aeruginosa Pil-Chp Chemosensory System

Silversmith¹,

Wang

Fulcher

et al. 2016

Journal of Biological Chemistry

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Bacterial chemosensory signal transduction systems that regulate motility by type IV pili (T4P) can be markedly more complex than related flagellum-based chemotaxis systems. In T4P-based systems, the CheA kinase often contains numerous potential sites of phosphorylation, but the signaling mechanisms of these systems are unknown. In Pseudomonas aeruginosa, the Pil-Chp system regulates T4P-mediated twitching motility and cAMP levels, both of which play roles in pathogenesis. The Pil-Chp histidine kinase (ChpA) has eight "Xpt" domains; six are canonical histidine-containing phosphotransfer (Hpt) domains and two have a threonine (Tpt) or serine (Spt) in place of the histidine. Additionally, there are two stand-alone receiver domains (PilG and PilH) and a ChpA C-terminal receiver domain (ChpArec). Here, we demonstrate that the ChpA Xpts are functionally divided into three categories as follows: (i) those phosphorylated with ATP (Hpt4 -6); (ii) those reversibly phosphorylated by ChpArec (Hpt2-6), and (iii) those with no detectable phosphorylation (Hpt1, Spt, and Tpt). There was rapid phosphotransfer from Hpt2-6 to ChpArec and from Hpt3 to PilH, whereas transfer to PilG was slower. ChpArec also had a rapid rate of autodephosphorylation. The biochemical results together with in vivo cAMP and twitching phenotypes of key ChpA phosphorylation site point mutants supported a scheme whereby ChpArec functions both as a phosphate sink and a phosphotransfer element linking Hpt4 -6 to Hpt2-3. Hpt2 and Hpt3 are likely the dominant sources of phosphoryl groups for PilG and PilH, respectively. The data are synthesized in a signaling circuit that contains fundamental features of twocomponent phosphorelays.

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Functional roles of conserved amino acid residues surrounding the phosphorylatable histidine of the yeast phosphorelay protein YPD1

Cited by 40 publications

References 28 publications

Crystal Structure of the CheA Histidine Phosphotransfer Domain that Mediates Response Regulator Phosphorylation in Bacterial Chemotaxis

Crystal Structure of the CheA Histidine Phosphotransfer Domain that Mediates Response Regulator Phosphorylation in Bacterial Chemotaxis

Osmotic Stress Signaling and Osmoadaptation in Yeasts

Phosphoryl Group Flow within the Pseudomonas aeruginosa Pil-Chp Chemosensory System

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