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Cell Oct 2021Being able to precisely turn on or off particular neurons in the brain at will was a major challenge for the neuroscience field, and few could have anticipated that the...
Being able to precisely turn on or off particular neurons in the brain at will was a major challenge for the neuroscience field, and few could have anticipated that the solution would come from algae. The 2021 Albert Lasker Basic Medical Research Award recognizes the contributions of Peter Hegemann, Dieter Oesterhelt, and Karl Deisseroth for their discovery of light-sensitive microbial proteins that can activate or silence brain cells. Cell editor Nicole Neuman had a conversation with Peter Hegemann about his role in bridging the two fields of microbial phototaxis and neuroscience and his perspective on the nature and future of interdisciplinary science. Excerpts from this conversation are presented below, and the full conversation is available with the article online.
Topics: Awards and Prizes; Bacterial Proteins; Bacteriorhodopsins; Channelrhodopsins; Humans; Light; Optogenetics
PubMed: 34562361
DOI: 10.1016/j.cell.2021.08.009 -
Nature Neuroscience Sep 2015Over the past 10 years, the development and convergence of microbial opsin engineering, modular genetic methods for cell-type targeting and optical strategies for... (Review)
Review
Over the past 10 years, the development and convergence of microbial opsin engineering, modular genetic methods for cell-type targeting and optical strategies for guiding light through tissue have enabled versatile optical control of defined cells in living systems, defining modern optogenetics. Despite widespread recognition of the importance of spatiotemporally precise causal control over cellular signaling, for nearly the first half (2005-2009) of this 10-year period, as optogenetics was being created, there were difficulties in implementation, few publications and limited biological findings. In contrast, the ensuing years have witnessed a substantial acceleration in the application domain, with the publication of thousands of discoveries and insights into the function of nervous systems and beyond. This Historical Commentary reflects on the scientific landscape of this decade-long transition.
Topics: Animals; Bacteriorhodopsins; Humans; Light; Neurosciences; Opsins; Optogenetics; Photic Stimulation; Protein Structure, Secondary; Rhodopsins, Microbial
PubMed: 26308982
DOI: 10.1038/nn.4091 -
Biotechnology Advances 2021Archaea are a domain of prokaryotic organisms with intriguing physiological characteristics and ecological importance. In Microbial Biotechnology, archaea are... (Review)
Review
Archaea are a domain of prokaryotic organisms with intriguing physiological characteristics and ecological importance. In Microbial Biotechnology, archaea are historically overshadowed by bacteria and eukaryotes in terms of public awareness, industrial application, and scientific studies, although their biochemical and physiological properties show a vast potential for a wide range of biotechnological applications. Today, the majority of microbial cell factories utilized for the production of value-added and high value compounds on an industrial scale are bacterial, fungal or algae based. Nevertheless, archaea are becoming ever more relevant for biotechnology as their cultivation and genetic systems improve. Some of the main advantages of archaeal cell factories are the ability to cultivate many of these often extremophilic organisms under non-sterile conditions, and to utilize inexpensive feedstocks often toxic to other microorganisms, thus drastically reducing cultivation costs. Currently, the only commercially available products of archaeal cell factories are bacterioruberin, squalene, bacteriorhodopsin and diether-/tetraether-lipids, all of which are produced utilizing halophiles. Other archaeal products, such as carotenoids and biohydrogen, as well as polyhydroxyalkanoates and methane are in early to advanced development stages, respectively. The aim of this review is to provide an overview of the current state of Archaea Biotechnology by describing the actual state of research and development as well as the industrial utilization of archaeal cell factories, their role and their potential in the future of sustainable bioprocessing, and to illustrate their physiological and biotechnological potential.
Topics: Archaea; Bacteria; Biotechnology; Fungi; Industrial Microbiology; Polyhydroxyalkanoates
PubMed: 33271237
DOI: 10.1016/j.biotechadv.2020.107668 -
Frontiers in Molecular Biosciences 2015Rhodopsins are light-sensing proteins used in optogenetics. The word "rhodopsin" originates from the Greek words "rhodo" and "opsis," indicating rose and sight,... (Review)
Review
Rhodopsins are light-sensing proteins used in optogenetics. The word "rhodopsin" originates from the Greek words "rhodo" and "opsis," indicating rose and sight, respectively. Although the classical meaning of rhodopsin is the red-colored pigment in our eyes, the modern meaning of rhodopsin encompasses photoactive proteins containing a retinal chromophore in animals and microbes. Animal and microbial rhodopsins possess 11-cis and all-trans retinal, respectively, to capture light in seven transmembrane α-helices, and photoisomerizations into all-trans and 13-cis forms, respectively, initiate each function. Ion-transporting proteins can be found in microbial rhodopsins, such as light-gated channels and light-driven pumps, which are the main tools in optogenetics. Light-driven pumps, such as archaeal H(+) pump bacteriorhodopsin (BR) and Cl(-) pump halorhodopsin (HR), were discovered in the 1970s, and their mechanism has been extensively studied. On the other hand, different kinds of H(+) and Cl(-) pumps have been found in marine bacteria, such as proteorhodopsin (PR) and Fulvimarina pelagi rhodopsin (FR), respectively. In addition, a light-driven Na(+) pump was found, Krokinobacter eikastus rhodopsin 2 (KR2). These light-driven ion-pumping microbial rhodopsins are classified as DTD, TSA, DTE, NTQ, and NDQ rhodopsins for BR, HR, PR, FR, and KR2, respectively. Recent understanding of ion-pumping microbial rhodopsins is reviewed in this paper.
PubMed: 26442282
DOI: 10.3389/fmolb.2015.00052 -
Sensors (Basel, Switzerland) Apr 2018Bacteriorhodopsin protein extracted from is widely used in many biohybrid electronic devices and forms a research subject known as bioelectronics, which merges biology... (Review)
Review
Bacteriorhodopsin protein extracted from is widely used in many biohybrid electronic devices and forms a research subject known as bioelectronics, which merges biology with electronic technique. The specific molecule structure and components of bR lead to its unique photocycle characteristic, which consists of several intermediates (bR, K, L, M, N, and O) and results in proton pump function. In this review, working principles and properties of bacteriorhodopsin are briefly introduced, as well as bR layer preparation method. After that, different bR-based devices divided into photochemical and photoelectric applications are shown. Finally, outlook and conclusions are drawn to inspire new design of high-performance bR-based biohybrid electronic devices.
PubMed: 29702621
DOI: 10.3390/s18051368 -
Biophysical Reviews Feb 2023Gobind Khorana's distinguished career spanned nearly six decades (1952-2011). His work resulted in remarkable achievements starting with the complicated synthesis of...
Gobind Khorana's distinguished career spanned nearly six decades (1952-2011). His work resulted in remarkable achievements starting with the complicated synthesis of coenzyme A. He then pioneered the synthesis of DNA oligonucleotides, which enabled him to crack the genetic code. Using this experience, he ventured to accomplish the first complete synthesis of a gene. Not satisfied with elucidating the function of bacteriorhodopsin, Gobind took up another greater challenge, that of spearheading studies on visual rhodopsin, its mechanism of activation, and the consequent signal transduction pathway. This Editorial acts to introduce the articles appearing in this Issue Focus dedicated to celebrating the 100th anniversary of the year of his birth.
PubMed: 36909957
DOI: 10.1007/s12551-023-01045-w -
Cell Oct 2021The field of optogenetics realizes a dream first articulated by Francis Crick in the 1970s: to use light to turn specific neurons on (or off), so as to tease apart brain...
The field of optogenetics realizes a dream first articulated by Francis Crick in the 1970s: to use light to turn specific neurons on (or off), so as to tease apart brain function and mechanisms. Few could have anticipated that the technical solution to this grand neurobiology challenge would come from basic studies in Archaea and algae. The 2021 Albert Lasker Basic Medical Research Award recognizes the contributions of Dieter Oesterhelt, Peter Hegemann, and Karl Deisseroth for their discovery of microbial light-sensing proteins that can activate or silence individual brain cells and for their use in developing optogenetics, which has revolutionized neuroscience. Cell's Nicole Neuman had a conversation with Dieter Oesterhelt about his startling discovery that Archaea also possess rhodopsins, how this led to many other discoveries and technologies, and his experiences in cultivating scientific talent such as fellow award-winner Peter Hegemann. Excerpts from this conversation are presented below, and the full conversation is available with the article online.
Topics: Awards and Prizes; Bacteria; Bacteriorhodopsins; Humans; Light; Optogenetics; Pigmentation
PubMed: 34562366
DOI: 10.1016/j.cell.2021.08.011 -
Bosnian Journal of Basic Medical... Nov 2019Optogenetics is an emerging field, which uses light and molecular genetics to manipulate the activity of live cells by expressing light-sensitive proteins. With the... (Review)
Review
Optogenetics is an emerging field, which uses light and molecular genetics to manipulate the activity of live cells by expressing light-sensitive proteins. With the discovery of bacteriorhodopsin, a light-sensitive bacterial protein, in 1971 Oesterhelt and Stoeckenius laid the pavement of optogenetics. However, the cross-integration of different disciplines is a little more than a decade old. The toolbox contains fluorescent sensors and optogenetic actuators that enable visualization of signaling events and manipulation of cellular activities, respectively. Neuropathic pain is pain caused either by damage or disease that affects the somatosensory system. The exact mechanism for neuropathic pain is not known, however proposed mechanisms include immune reactions, ion channel expressions, and inflammation. Current regimen for the disease provides about 50% relief for only 40-60% of patients. Recent in vivo and in vitro studies demonstrate the potential therapeutic applications of optogenetics by manipulating the activity of neurons. This review summarizes the basic concept, therapeutic applications for neuropathy, and potential of optogenetics to reach from bench to bedside in the near future.
Topics: Agnosia; Animals; Bacteriorhodopsins; Blood-Brain Barrier; Chronic Pain; Epigenesis, Genetic; Humans; Inflammation; Interdisciplinary Research; Ion Channels; Light; Neuralgia; Neurons; Optogenetics; Pain Management; Retinitis Pigmentosa; Signal Transduction
PubMed: 30995901
DOI: 10.17305/bjbms.2019.4114 -
RSC Advances Feb 2023Rhodopsins, a family of photoreceptive membrane proteins, contain retinal as a chromophore and were firstly identified as reddish pigments from frog retina in 1876.... (Review)
Review
Rhodopsins, a family of photoreceptive membrane proteins, contain retinal as a chromophore and were firstly identified as reddish pigments from frog retina in 1876. Since then, rhodopsin-like proteins have been identified mainly from animal eyes. In 1971, a rhodopsin-like pigment was discovered from the archaeon and named bacteriorhodopsin. While it was believed that rhodopsin- and bacteriorhodopsin-like proteins were expressed only in animal eyes and archaea, respectively, before the 1990s, a variety of rhodopsin-like proteins (called animal rhodopsins or opsins) and bacteriorhodopsin-like proteins (called microbial rhodopsins) have been progressively identified from various tissues of animals and microorganisms, respectively. Here, we comprehensively introduce the research conducted on animal and microbial rhodopsins. Recent analysis has revealed that the two rhodopsin families have common molecular properties, such as the protein structure (, 7-transmembrane structure), retinal structure (, binding ability to - and -retinal), color sensitivity (, UV- and visible-light sensitivities), and photoreaction (, triggering structural changes by light and heat), more than what was expected at the early stages of rhodopsin research. Contrastingly, their molecular functions are distinctively different (, G protein-coupled receptors and photoisomerases for animal rhodopsins and ion transporters and phototaxis sensors for microbial rhodopsins). Therefore, based on their similarities and dissimilarities, we propose that animal and microbial rhodopsins have convergently evolved from their distinctive origins as multi-colored retinal-binding membrane proteins whose activities are regulated by light and heat but independently evolved for different molecular and physiological functions in the cognate organism.
PubMed: 36793294
DOI: 10.1039/d2ra07073a -
Biochemistry. Biokhimiia Oct 2023The diversity of the retinal-containing proteins (rhodopsins) in nature is extremely large. Fundamental similarity of the structure and photochemical properties unites... (Review)
Review
The diversity of the retinal-containing proteins (rhodopsins) in nature is extremely large. Fundamental similarity of the structure and photochemical properties unites them into one family. However, there is still a debate about the origin of retinal-containing proteins: divergent or convergent evolution? In this review, based on the results of our own and literature data, a comparative analysis of the similarities and differences in the photoconversion of the rhodopsin of types I and II is carried out. The results of experimental studies of the forward and reverse photoreactions of the bacteriorhodopsin (type I) and visual rhodopsin (type II) rhodopsins in the femto- and picosecond time scale, photo-reversible reaction of the octopus rhodopsin (type II), photovoltaic reactions, as well as quantum chemical calculations of the forward photoreactions of bacteriorhodopsin and visual rhodopsin are presented. The issue of probable convergent evolution of type I and type II rhodopsins is discussed.
Topics: Rhodopsin; Bacteriorhodopsins; Photochemistry
PubMed: 38105022
DOI: 10.1134/S0006297923100097