Two-Component Signal Transduction

Article Properties
  • Language
    English
  • Publication Date
    2000/06/01
  • Indian UGC (Journal)
  • Refrences
    281
  • Citations
    2,320
  • Ann M. Stock Center for Advanced Biotechnology and Medicine and Howard Hughes Medical Institute, University of Medicine and Dentistry of New Jersey-Robert Wood Johnson Medical School, Piscataway, New Jersey 08854;
  • Victoria L. Robinson Center for Advanced Biotechnology and Medicine and Howard Hughes Medical Institute, University of Medicine and Dentistry of New Jersey-Robert Wood Johnson Medical School, Piscataway, New Jersey 08854;
  • Paul N. Goudreau Center for Advanced Biotechnology and Medicine and Howard Hughes Medical Institute, University of Medicine and Dentistry of New Jersey-Robert Wood Johnson Medical School, Piscataway, New Jersey 08854;
Abstract
Cite
Stock, Ann M., et al. “Two-Component Signal Transduction”. Annual Review of Biochemistry, vol. 69, no. 1, 2000, pp. 183-15, https://doi.org/10.1146/annurev.biochem.69.1.183.
Stock, A. M., Robinson, V. L., & Goudreau, P. N. (2000). Two-Component Signal Transduction. Annual Review of Biochemistry, 69(1), 183-215. https://doi.org/10.1146/annurev.biochem.69.1.183
Stock AM, Robinson VL, Goudreau PN. Two-Component Signal Transduction. Annual Review of Biochemistry. 2000;69(1):183-215.
Journal Categories
Science
Biology (General)
Science
Chemistry
Organic chemistry
Biochemistry
Description

How do bacteria sense and respond to their environment? This review provides a comprehensive overview of two-component signal transduction systems, a widespread mechanism in prokaryotes and some eukaryotic pathways. These systems involve a histidine protein kinase and a response regulator protein, which work together to detect and respond to environmental stimuli. The review elucidates the phosphotransfer scheme, where the histidine protein kinase autophosphorylates at a histidine residue, subsequently transferring the phosphoryl group to an aspartate residue in the response regulator. This phosphorylation event triggers a conformational change, activating a domain that mediates the response. Two-component systems are highly adaptable, allowing for optimization within specific signaling contexts. The modular nature of these proteins allows for versatile integration into diverse pathways, while maintaining core functions. Detailed analyses of representative proteins offer a foundation for understanding this extensive family of signaling proteins, providing insights into bacterial adaptation and survival. This review is of particular importance to those interested in the evolution of the cellular responses.

As a review published in Annual Review of Biochemistry, this article fits well within the journal’s scope of providing comprehensive and critical assessments of significant advances in biochemistry and molecular biology. The review on two-component signal transduction offers valuable insights for researchers in various fields.

Refrences
Citations
Citations Analysis
The first research to cite this article was titled The Phosphoryl Transfer Domain of UhpB Interacts with the Response Regulator UhpA and was published in 2001. The most recent citation comes from a 2024 study titled The Phosphoryl Transfer Domain of UhpB Interacts with the Response Regulator UhpA . This article reached its peak citation in 2017 , with 133 citations.It has been cited in 533 different journals, 21% of which are open access. Among related journals, the Journal of Bacteriology cited this research the most, with 204 citations. The chart below illustrates the annual citation trends for this article.
Citations used this article by year