Abiotic Regulation: A Common Way for Proteins to Modulate their Functions

Title:Abiotic Regulation: A Common Way for Proteins to Modulate their Functions

Volume: 16 Issue: 3

Author(s): Zhi Zou and Xinmiao Fu

Affiliation:

Keywords: Abiotic factor, abiotic regulation, allosteric regulation, covalent modification, protein intrinsic activity, proteinprotein interaction.

Abstract: Modulation of protein intrinsic activity in cells is generally carried out via a combination of four common ways, i.e., allosteric regulation, covalent modification, proteolytic cleavage and association of other regulatory proteins. Accumulated evidence indicate that changes of certain abiotic factors (e.g., temperature, pH, light and mechanical force) within or outside the cells directly influence protein structure and thus profoundly modulate the functions of a wide range of proteins, termed as abiotic regulatory proteins (e.g., heat shock factor, small heat shock protein, hemoglobin, zymogen, integrin, rhodopsin). Such abiotic regulation apparently differs from the four classic ways in perceiving and response to the signals. Importantly, it enables cells to directly and also immediately response to extracellular stimuli, thus facilitating the ability of organisms to resist against and adapt to the abiotic stress and thereby playing crucial roles in life evolution. Altogether, abiotic regulation may be considered as a common way for proteins to modulate their functions.

Cite this article as:

Zou Zhi and Fu Xinmiao, Abiotic Regulation: A Common Way for Proteins to Modulate their Functions, Current Protein & Peptide Science 2015; 16 (3) . https://dx.doi.org/10.2174/1389203716666150224124429