Bulbus arteriosus of the antarctic teleosts. I. The white-blooded Chionodraco hamatus.
The bulbus arteriosus of teleost fish is a thick-walled chamber that extends between the single ventricle and the ventral aorta. The functional importance of the bulbus resides in the fact that it maintains a steady blood flow into the gill system through heart contraction. Despite of this, a thorough study of the structure of the bulbus in teleost fish is still lacking. We have undertaken a morphologic study of the bulbus arteriosus in the stenothermal teleosts of the Antarctic sea. The structural organization of the bulbus arteriosus of the icefish Chionodraco hamatus has been studied here by conventional light, scanning, and transmission electron microscopy. The inner surface of the bulbus shows a festooned appearance due to the presence of longitudinal, unbranched ridges that extend between the ventricle and the arterial trunk. The wall of the bulbus is divided into endocardial, subendocardial, middle, and external layers. Endocardial cells show a large number of moderately-dense bodies. The endocardium invaginates into the subendocardium forming solid epithelial cords that contain numerous secretory vacuoles. Cells in the subendocardium group into small domains, have some of the morphological characteristics of smooth muscle cells, and appear enmeshed in a three-dimensional network of matrix filaments. Cells in the middle layer are typical smooth muscle cells. They appear arranged into layers and are surrounded by a filamentous meshwork that excludes collagen fibers. Orientation of this meshwork occurs in the vicinity of the smooth muscle cells. Elastin fibers are never observed. The external layer is formed by wavy collagen bundles and fibroblast-like cells. This layer lacks blood vessels and nerve fibers. The endocardium and the endocardium-derived cords are secretory epithelia that may be involved in the formation ofmucins or glycosaminoglycans. These mucins may have a protecting effect on the endocardium. The subendocardium and the middle layer appear to be formed by the same cell type, smooth muscle, with a gradient of differentiation from the secretory (subendocardium) to the contractile (middle layer) phenotype. Despite the absence of elastin fibers, the filamentous matrix could maintain the elastic properties of the bulbus wall. Smooth muscle cells appear to be actively involved in bulbus wall dynamics. The restriction of collagen to the external layer suggests that it may control wall dilatation and bulbus compliance. When comparison was possible, structural differences between C. hamatus and temperate teleosts seemed to be not species-related, but of phenotypic adaptative significance. This is remarkable since Antarctic fishes have lived isolated in freezing waters for the last two million years. (+info)
Prolonged eradication of urogenital mycoplasmas after administration of tetracycline to men in the Antarctic.
Meatal swabs were obtained at intervals over 1 year from 23 men in the Antarctic. A 5-day course of tetracycline was given to twelve of them. In retrospect it was found that the antibiotic had been received by two men who were harbouring ureaplasmas, one of whom also had M. hominis. After treatment, these organisms were not found in any of the swabs taken over the next year, except in a swab from one of the men following sexual contact after this time. One of the twelve men developed N.S.U. just before arriving in the Antarctic. He responded clinically to a shorter course of tetracycline and ureplasmas were not recovered from a meatal swab immediately thereafter. However, without further sexual contact, ureaplasmas and disease recurred about a month later. This time, after a 5-day course of tetracycline, disease was not seen, and ureaplasmas were not isolated, over the next year. In contrast, ureaplasmas were isolated consistently over a year from two men who were not given the antibiotic. The evidence strongly suggests that, under natural conditions, the most likely cause of mycoplasmas, particularly ureaplasmas, recurring in the genital tract after apparently adequate tetracycline therapy, is re-infection as a result of sexual re-exposure. (+info)
A RNA polymerase with transcriptional activity at 0 degrees C from the Antarctic bacterium Pseudomonas syringae.
A DNA-dependent RNA polymerase was purified from the Antarctic psychrotrophic bacterium Pseudomonas syringae. The RNA polymerase showed a typical eubacterial subunit composition with beta, beta', alpha2 and sigma subunits. The subunits cross-reacted with antibodies raised against holoenzyme and the individual subunits of the RNA polymerase of Escherichia coli. However, the enzyme was considered unique, since unlike the RNA polymerase of mesophilic E. coli it exhibited significant and consistent transcriptional activity (10-15%) even at 0 degrees C. But, similar to the enzyme from the mesophilic bacterium, the RNA polymerase from P. syringae exhibited optimum activity at 37 degrees C. The study also demonstrates that the RNA polymerase of P. syringae could preferentially transcribe the cold-inducible gene cspA of E. coli only at lower temperatures (0-22 degrees C). The polymerase was also observed to be relatively more rifampicin-resistant during transcription at lower temperature. (+info)
Metallothioneins in antarctic fish: evidence for independent duplication and gene conversion.
In the present paper, we examine eight species of Antarctic fish belonging to the suborder Notothenioidei, using reverse-transcriptase polymerase chain reaction, to investigate the presence of mRNAs encoding metallothionein (MT) isoforms. A total of 168 bp from the coding region and the complete (133-165 bp) 3' untranslated region (UTR) was obtained for all species (for three of them, we also sequenced the full-length cDNA, including the 5' UTR). Phylogenetic analyses carried out on the MT-coding region suggest monophyly for Antarctic fish MTs with respect to other teleost MT genes. Analyses also revealed that notothenioid MTs can be divided into at least two groups of paralogy, MT-1 and MT-2. These results indicate that notothenioid MT isoforms arose from at least one gene duplication event occurring in the ancestral lineage of the Notothenioidei. This duplication occurred independent of the one which gave origin to two metallothionein isoforms in the rainbow trout. In addition, an instance of gene conversion was observed between MT-1 and MT-2 genes in Notothenia coriiceps. Analyses of the 5' UTR, combined with quantitative assay of differential expression of MT-1 and MT-2, indicate that only the 3' UTR underwent a gene conversion event in the mentioned species. These findings, together with the observation of a differential pattern of expression for the two MT isoforms, disclose an unexpected complexity in the evolution and function of notothenioid MTs; as in most teleost species examined (apart from the rainbow trout), a single MT form is present. (+info)
Determination of the solution structure of the N-domain plus linker of Antarctic eel pout antifreeze protein RD3.
RD3, a new antifreeze protein (AFP) extracted from antarctic eel pout is a single polypeptide divided into homologous N-terminal (residues Asn(1)-Glu(64)) and C-terminal (residues Ser(74)-Glu(134)) domains, each of which has a high sequence identity with Type III AFP. A 9-residue linker (-D(65)GTTSPGLK(73)-) connects these two domains in tandem and is thought to play a significant role in defining the nature of the intact molecule. The present paper shows for the first time the solution structure and preliminary (15)N-NMR backbone dynamics data of the N-domain plus the linker of recombinant RD3 protein (RD3-Nl: residues 1-73) by employing homo- and heteronuclear multidimensional NMR spectroscopy. Forty converged structures of RD3-Nl were successfully calculated by using a total of 958 NMR-derived structural restraints. It was found that the N-domain of RD3-Nl has a globular form comprising six beta-strands, three type III turns, and several loops, which stabilize a flat, ice-binding site formed on one side of this domain. Further, the linker portion appears to have a definitive structure, which is independent of the globular N-domain. This definitive linker is roughly divided into two short strands, -D(65)GTTSP(70)- and -G(71)LK(73)-, which are bent around -T(67)TSPG(71)- at an angle of approximately 60 degrees. This bending motif of the linker may function to orient the two ice-binding sites of the N- and C-domains of RD3 in the same direction, leading to their simultaneous interactions with the ice crystal surface. (+info)
Physicochemical parameters for growth of the sea ice bacteria Glaciecola punicea ACAM 611(T) and Gelidibacter sp. strain IC158.
The water activity and pH ranges for growth of Glaciecola punicea (a psychrophile) were extended when this organism was grown at suboptimal rather than optimal temperatures. No such extension was observed for Gelidibacter sp. strain IC158 (a psychrotolerant bacterium) at analogous temperatures. Salinity and pH may be primary physicochemical parameters controlling bacterial community development in sea ice. (+info)
Temperature-dependent expression of cytochrome-c oxidase in Antarctic and temperate fish.
Seasonal acclimation versus permanent adaptation to low temperatures leads to a differential response in the expression of cytochrome-c oxidase (CCO) in temperate and Antarctic eelpouts. Although eurythermal eelpout from the North Sea (Zoarces viviparus) displayed a cold-induced rise of CCO activity in white muscle, enzyme activity in the cold stenothermal Antarctic eelpout Pachycara brachycephalum failed to reflect such a compensatory increase. In Antarctic eelpout, CCO activity correlates with transcript levels of mitochondrial encoded subunits of CCO (CCO I and CCO II), whereas cold-acclimated eelpout from the North Sea show lower enzyme activities than expected on the basis of mitochondrial mRNA levels. In these animals, CCO expression at low temperatures may be limited either by nuclear CCO transcripts or by posttranscriptional processes. These may comprise translation of the subunits or assembly of the CCO holoenzyme. mRNA levels of CCO IV, one of the nuclear encoded subunits, increased strongly during cold acclimation, indicating that the expression of CCO is likely not message limited in cold-acclimated Z. viviparus. Our data suggest that seasonal cold acclimation of Z. viviparus results in a modification of the relationship between transcription and translation or posttranslational processes. In permanently cold-adapted P. brachycephalum, on the other hand, CCO expression shows similar characteristics as in the warm-acclimated confamilial species, e.g., low levels of enzyme activity correlated with low levels of mitochondrial message. (+info)
Cold-adapted alanine dehydrogenases from two antarctic bacterial strains: gene cloning, protein characterization, and comparison with mesophilic and thermophilic counterparts.
The genes encoding NAD(+)-dependent alanine dehydrogenases (AlaDHs) (EC 126.96.36.199) from the Antarctic bacterial organisms Shewanella sp. strain Ac10 (SheAlaDH) and Carnobacterium sp. strain St2 (CarAlaDH) were cloned and expressed in Escherichia coli. Of all of the AlaDHs that have been sequenced, SheAlaDH exhibited the highest level of sequence similarity to the AlaDH from the gram-negative bacterium Vibrio proteolyticus (VprAlaDH). CarAlaDH was most similar to AlaDHs from mesophilic and thermophilic Bacillus strains. SheAlaDH and CarAlaDH had features typical of cold-adapted enzymes; both the optimal temperature for catalytic activity and the temperature limit for retaining thermostability were lower than the values obtained for the mesophilic counterparts. The k(cat)/K(m) value for the SheAlaDH reaction was about three times higher than the k(cat)/K(m) value for VprAlaDH, but it was much lower than the k(cat)/K(m) value for the AlaDH from Bacillus subtilis. Homology-based structural models of various AlaDHs, including the two psychotropic AlaDHs, were constructed. The thermal instability of SheAlaDH and CarAlaDH may result from relatively low numbers of salt bridges in these proteins. (+info)