title: The molecular chaperone system and other anti-stress mechanisms in archaea.
abstract: This article presents a brief review of stressors, their cellular and intracellular targets, stress proteins, molecular chaperones, and other anti-stress mechanisms. New data are reported on cochaperones and multicellular structures in archaea. The molecular chaperoning systems of bacteria and eukaryotes have been studied for many years and are relatively well known in terms of their components and mechanisms of action, although many details remain to be elucidated and almost certainly other components will be discovered in the future. By comparison, the molecular chaperoning system of archaea is still unexplored. Since archaea have some molecular genetic and physiologic features similar to those of bacteria and some resembling those of eukaryotes, extrapolation from what is known of organisms from these two phylogenetic domains to archaeal species is unwarranted. For example, the components of the molecular chaperone machine, Hsp70(DnaK), Hsp40(DnaJ), and GrpE, in the archaeal species that have it, are closely related to bacterial counterparts, whereas the archaeal chaperonins are like the eukaryotic equivalents. Furthermore, many archaeal species lack the chaperone machine, in contrast to bacteria and eukaryotes that have it without any known exception. A search for the cochaperones trigger factor, Hop, Hip, BAG-1, and NAC in archaeal genomes demonstrated no conserved equivalents, but two families of archaeal molecules were identified that might be related to NAC and Hop, respectively. Multicellular structures with a single species such as packet and lamina are formed by Methanosarcina species, among which the best studied is M. mazeii. Multispecies multicellular structures are formed by a variety of archaeal organisms, which are either flat (biofilm) or globular (granule) and constitute a functional association or consortium. Details of morphology, formation, and internal organization are described for representative examples of multicellular structures. These may be seen as the result of primitive histogenesis reflecting primeval mechanisms of differentiation-development that might have evolved driven by environmental stressors. Cells in these complex threedimensional arrangements are not only positioned so they can interact with each other for more efficient functioning as in a tissue or organ, but are also protected from stressors. Single cells lacking the protective shield of other cells packed together with intercellular connective material, which is typical of multicellular structures, are directly exposed to environmental stressors and, thus, are at a disadvantage from the evolutionary standpoint. It seems reasonable to argue that differentiation-development leading to histogenesis might have arisen in primeval times as a consequence of the harsh conditions that primitive life forms had to endure, and that the ability to form tissue-like structures was a primary characteristic that ensured positive selection.
authors.affiliation: Wadsworth Center, New York State Department of Health, School of Public Health, The University at Albany (SUNY); Albany, New York, USA. macario@wadsworth.org
authors.forename: A J
authors.initials: AJ
authors.lastname: Macario
authors.forename: E
authors.initials: E
authors.lastname: Conway De Macario
mesh_terms: D000209:Acute-Phase Proteins / Q000378:metabolism; D000222:Adaptation, Physiological; D000818:Animals; D000951:Antigens, Neoplasm; D017209:Apoptosis / Q000502:physiology; D001105:Archaea / Q000166:cytology / Q000502:physiology*; D001426:Bacterial Proteins; D018441:Biofilms; D014408:Biomarkers, Tumor; D019149:Bioreactors; D002352:Carrier Proteins / Q000378:metabolism; D002454:Cell Differentiation; D004268:DNA-Binding Proteins / Q000378:metabolism; D029721:Drosophila Proteins; D029968:Escherichia coli Proteins; D005109:Extracellular Matrix / Q000502:physiology; D005656:Fungal Proteins / Q000378:metabolism; D006360:Heat-Shock Proteins / Q000378:metabolism*; D053612:Janus Kinases; D037181:Lectins, C-Type; D018832:Molecular Chaperones / Q000378:metabolism*; D000073718:Pancreatitis-Associated Proteins; D019696:Peptidylprolyl Isomerase / Q000378:metabolism; D011387:Prokaryotic Cells / Q000378:metabolism; D011505:Protein-Tyrosine Kinases / Q000378:metabolism; D013314:Stress, Mechanical; D014157:Transcription Factors / Q000378:metabolism
chemical_list: D000209:Acute-Phase Proteins; D000951:Antigens, Neoplasm; C091732:BCL2-associated athanogene 1 protein; D001426:Bacterial Proteins; D014408:Biomarkers, Tumor; D002352:Carrier Proteins; D004268:DNA-Binding Proteins; D029721:Drosophila Proteins; D029968:Escherichia coli Proteins; D005656:Fungal Proteins; D006360:Heat-Shock Proteins; D037181:Lectins, C-Type; D018832:Molecular Chaperones; C072712:NAC protein, bacteria; C489526:Nac protein, E coli; D000073718:Pancreatitis-Associated Proteins; D014157:Transcription Factors; C112806:prefoldin; D011505:Protein-Tyrosine Kinases; D053612:Janus Kinases; C085845:hop protein, Drosophila; C403324:trigger factor, E coli; D019696:Peptidylprolyl Isomerase