skip to main content
OSTI.GOV title logo U.S. Department of Energy
Office of Scientific and Technical Information

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

Abstract

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.

Authors:
 [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)
Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States)
Sponsoring Org.:
National Science Foundation (NSF); USDOE
OSTI Identifier:
1494700
Grant/Contract Number:  
AC02-06CH11357
Resource Type:
Journal Article: Accepted Manuscript
Journal Name:
BMC Biochemistry (Online)
Additional Journal Information:
Journal Volume: 20; Journal Issue: 1; Journal ID: ISSN 1471-2091
Publisher:
BioMed Central
Country of Publication:
United States
Language:
English
Subject:
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

Citation Formats

Kennedy, Emily N., Hebdon, Skyler D., Menon, Smita K., Foster, Clay A., Copeland, Daniel M., Xu, Qingping, Janiak-Spens, Fabiola, and West, Ann H. Role of the highly conserved G68 residue in the yeast phosphorelay protein Ypd1: implications for interactions between histidine phosphotransfer (HPt) and response regulator proteins. United States: N. p., 2019. Web. doi:10.1186/s12858-019-0104-5.
Kennedy, Emily N., Hebdon, Skyler D., Menon, Smita K., Foster, Clay A., Copeland, Daniel M., Xu, Qingping, Janiak-Spens, Fabiola, & West, Ann H. Role of the highly conserved G68 residue in the yeast phosphorelay protein Ypd1: implications for interactions between histidine phosphotransfer (HPt) and response regulator proteins. United States. doi:10.1186/s12858-019-0104-5.
Kennedy, Emily N., Hebdon, Skyler D., Menon, Smita K., Foster, Clay A., Copeland, Daniel M., Xu, Qingping, Janiak-Spens, Fabiola, and West, Ann H. Mon . "Role of the highly conserved G68 residue in the yeast phosphorelay protein Ypd1: implications for interactions between histidine phosphotransfer (HPt) and response regulator proteins". United States. doi:10.1186/s12858-019-0104-5. https://www.osti.gov/servlets/purl/1494700.
@article{osti_1494700,
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},
author = {Kennedy, Emily N. and Hebdon, Skyler D. and Menon, Smita K. and Foster, Clay A. and Copeland, Daniel M. and Xu, Qingping and Janiak-Spens, Fabiola and West, Ann H.},
abstractNote = {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.},
doi = {10.1186/s12858-019-0104-5},
journal = {BMC Biochemistry (Online)},
issn = {1471-2091},
number = 1,
volume = 20,
place = {United States},
year = {2019},
month = {1}
}

Journal Article:
Free Publicly Available Full Text
Publisher's Version of Record

Citation Metrics:
Cited by: 1 work
Citation information provided by
Web of Science

Figures / Tables:

Fig. 1 Fig. 1: H + 4 residue relative to the phosphorylatable histidine is highly conserved. a Representative sequence alignment of the αC region of HPt proteins/domains from fungi, plants, and bacteria. The phosphorylatable histidine residue is highlighted in red, and the H + 4 residue is highlighted in blue. b Frequencymore » of residues found in positions surrounding the phosphorylatable histidine are represented by a WebLogo created using the complete sequence alignment. Indicated residue positions are based on the numbering of the S. cerevisiae Ypd1 HPt protein« less

Save / Share:

Works referenced in this record:

Fps1p controls the accumulation and release of the compatible solute glycerol in yeast osmoregulation
journal, February 1999


WebLogo: A Sequence Logo Generator
journal, May 2004

  • Crooks, Gavin E.; Hon, Gary; Chandonia, John-Marc
  • Genome Research, Vol. 14, Issue 6, p. 1188-1190
  • DOI: 10.1101/gr.849004