At the intersection of microbiology and biophysics, the study of microbial rhodopsins is receiving increasing attention. These rhodopsins are retinal-binding proteins that are primarily responsible for performing light-dependent ion transport and sensing functions in halophilic bacteria and other microorganisms. With in-depth study of these proteins, scientists are gradually unraveling the mystery of their evolution and thinking about their connection with animal rhodopsins.
Microbial rhodopsins are common in archaea and bacteria, but are relatively rare in complex multicellular organisms, which makes people wonder: Are they ancient witnesses of evolution in many organisms?
Microbial rhodopsins are mainly divided into several categories, including light-driven proton pumps, ion pumps and ion channels. The following are several well-known microbial rhodopsins and their corresponding functions:
The rhodopsins of these microorganisms obtain energy for the microorganisms or sense the environment through different mechanisms. These functions allow microbial rhodopsins to not only play key roles in ecosystems but also provide in-depth understanding of their evolution.
A striking fact about the evolution of rhodopsin is that all animal rhodopsins are derived from an ancient family of G protein-coupled receptors (GPCRs), but the sequence of microbial rhodopsins is identical to that of any GPCR Families vary greatly. This suggests that the origin and evolutionary pathway of microbial rhodopsin has a different history than that of animal rhodopsin.
Variations in microbial rhodopsins reflect their ability to adapt in various ecological niches, which leads us to wonder: Do these adaptations also provide microorganisms with some degree of survival advantage?
Microbial rhodopsin is usually composed of seven transmembrane helical structures, which provide the necessary framework for its light sensing and ion transport functions. Different subtypes of microbial rhodopsins may differ in their structure, but all maintain similar functional units. For example, the structure of bacteriorhodopsin allows it to transfer protons when excited by light.
While there are indeed structural and functional differences between microbial and animal rhodopsins, they also display some similarities. The evolution of animal rhodopsin appears to be through gene duplication and mutation, which is in sharp contrast to the evolution mechanism of microbial rhodopsin. This once again triggered thinking about the evolutionary origins of these different biological functions.
As a part of the evolution of life, microbial rhodopsin not only has remarkable effects in light perception and energy conversion, but its evolution process also provides the scientific community with rich research materials. Understanding how these microbial rhodopsins evolved and how they are related to animal rhodopsins will help us understand more fully the origin and evolution of life. So, will the diversity of these microbial rhodopsins bring new inspiration for future biotechnology?