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Title: Role of the highly conserved G68 residue in the yeast phosphorelay protein Ypd1: implications for interactions between histidine phosphotransfer (HPt) and response regulator proteins

Journal Article · · BMC Biochemistry (Online)
 [1];  [2];  [2];  [1];  [3];  [4];  [2]; ORCiD logo [2]
  1. Univ. of Oklahoma, Norman, OK (United States); Univ. of North Carolina, Chapel Hill, NC (United States)
  2. Univ. of Oklahoma, Norman, OK (United States)
  3. Univ. of Oklahoma, Norman, OK (United States); Pacira Pharmaceuticals, San Diego, CA (United States)
  4. Univ. of Oklahoma, Norman, OK (United States); Argonne National Lab. (ANL), Lemont, IL (United States)
+ Show Author Affiliations

Many bacteria and certain eukaryotes utilize multi-step His-to-Asp phosphorelays for adaptive responses to their extracellular environments. Histidine phosphotransfer (HPt) proteins function as key components of these pathways. HPt proteins are genetically diverse, but share a common tertiary fold with conserved residues near the active site. A surface-exposed glycine at the H + 4 position relative to the phosphorylatable histidine is found in a significant number of annotated HPt protein sequences. Furthermore previous reports demonstrated that substitutions at this position result in diminished phosphotransfer activity between HPt proteins and their cognate signaling partners.

Research Organization:
Argonne National Laboratory (ANL), Argonne, IL (United States)
Sponsoring Organization:
National Science Foundation (NSF); USDOE
Grant/Contract Number:
AC02-06CH11357
OSTI ID:
1494700
Journal Information:
BMC Biochemistry (Online), Vol. 20, Issue 1; ISSN 1471-2091
Publisher:
BioMed CentralCopyright Statement
Country of Publication:
United States
Language:
English
Citation Metrics:
Cited by: 4 works
Citation information provided by
Web of Science

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Cited By (2)

Modeling of Protein–Protein Interactions in Cytokinin Signal Transduction journal April 2019
Insights revealed by the co‐crystal structure of the Saccharomyces cerevisiae histidine phosphotransfer protein Ypd1 and the receiver domain of its downstream response regulator Ssk1 journal October 2019

Linked Research (4)

Figures / Tables (11)

Fig. 1(p. 3)figure Fig. 1
Table 1(p. 4)table Table 1
Table 2(p. 4)table Table 2
Fig. 2(p. 5)figure Fig. 2
Fig. 3(p. 5)figure Fig. 3
Fig. 4(p. 6)figure Fig. 4
Table 3(p. 6)table Table 3
Table 4(p. 7)table Table 4
Fig. 5(p. 8)figure Fig. 5
Fig. 6(p. 9)figure Fig. 6
Fig. 7(p. 10)figure Fig. 7

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Related Subjects

59 BASIC BIOLOGICAL SCIENCES
37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY
Two-component signal transduction
Ypd1
HPt proteins
Response regulator
Protein-protein interactions
Evolutionary conservation
Phosphotransfer