- Pigmented Marine Heterotrophic Bacteria: Occurrence, Diversity, and Characterization of Pigmentation

2013 ◽  
pp. 140-171 ◽  
2018 ◽  
Vol 475 (22) ◽  
pp. 3609-3628 ◽  
Author(s):  
Jonathan Dorival ◽  
Sophie Ruppert ◽  
Melissa Gunnoo ◽  
Adam Orłowski ◽  
Maylis Chapelais-Baron ◽  
...  

Cell walls of marine macroalgae are composed of diverse polysaccharides that provide abundant carbon sources for marine heterotrophic bacteria. Among them, Zobellia galactanivorans is considered as a model for studying algae–bacteria interactions. The degradation of typical algal polysaccharides, such as agars or alginate, has been intensively studied in this model bacterium, but the catabolism of plant-like polysaccharides is essentially uncharacterized. Here, we identify a polysaccharide utilization locus in the genome of Z. galactanivorans, induced by laminarin (β-1,3-glucans), and containing a putative GH5 subfamily 4 (GH5_4) enzyme, currently annotated as a endoglucanase (ZgEngAGH5_4). A phylogenetic analysis indicates that ZgEngAGH5_4 was laterally acquired from an ancestral Actinobacteria. We performed the biochemical and structural characterization of ZgEngAGH5_4 and demonstrated that this GH5 is, in fact, an endo-β-glucanase, most active on mixed-linked glucan (MLG). Although ZgEngAGH5_4 and GH16 lichenases both hydrolyze MLG, these two types of enzymes release different series of oligosaccharides. Structural analyses of ZgEngAGH5_4 reveal that all the amino acid residues involved in the catalytic triad and in the negative glucose-binding subsites are conserved, when compared with the closest relative, the cellulase EngD from Clostridium cellulovorans, and some other GH5s. In contrast, the positive glucose-binding subsites of ZgEngAGH5_4 are different and this could explain the preference for MLG, with respect to cellulose or laminarin. Molecular dynamics computer simulations using different hexaoses reveal that the specificity for MLG occurs through the +1 and +2 subsites of the binding pocket that display the most important differences when compared with the structures of other GH5_4 enzymes.


2021 ◽  
Author(s):  
Tao Wei ◽  
Caimeng Zhao ◽  
Mussa Quareshy ◽  
Nan Wu ◽  
Shen Huang ◽  
...  

In the marine environment, phosphorus availability significantly affects the lipid composition in many cosmopolitan marine heterotrophic bacteria, including members of the SAR11 clade and the Roseobacter clade. Under phosphorus stress conditions, non-phosphorus sugar-containing glycoglycerolipids are substitutes for phospholipids in these bacteria. Although these glycoglycerolipids play an important role as surrogates for phospholipids under phosphate deprivation, glycoglycerolipid synthases in marine microbes are poorly studied. In the present study, we biochemically characterized a glycolipid glycosyltransferase (GTcp) from the marine bacterium Candidatus Pelagibacter sp. HTCC7211, a member of the SAR11 clade. Our results showed that GTcp is able to act as a multifunctional enzyme by synthesizing different glycoglycerolipids with UDP-glucose, UDP-galactose, or UDP-glucuronic acid as sugar donors and diacylglycerol as the acceptor. Analyses of enzyme kinetic parameters demonstrated that Mg2+ notably changes the enzyme's affinity for UDP-glucose, which improves its catalytic efficiency. Homology modelling and mutational analyses revealed binding sites for the sugar donor and the diacylglycerol lipid acceptor, which provided insights into the retaining mechanism of GTcp with its GT-B fold. A phylogenetic analysis showed that GTcp and its homologs form a group in the GT4 glycosyltransferase family. These results not only provide new insights into the glycoglycerolipid synthesis mechanism in lipid remodelling, but also describe an efficient enzymatic tool for future synthesis of bioactive molecules.


Author(s):  
Kesi Kurnia ◽  
Nina Hermayani Sadi ◽  
Syafitri Jumianto

<span>Pollution of water environment with heavy metals is becoming one of the most severe environmental and human health hazards. Lead (Pb) is a major pollutant and highly toxic to human, animals, plants, and microbes. </span><span lang="IN">Toxic metals are difficult to remove from the environment, since they cannot be chemically or biologically degraded and are ultimately indestructible. Biological approaches based on metal-resistant microorganisms have received a great deal of attention as alternative remediation processes. </span><span>This study aim to isolat</span><span lang="IN">e</span><span> and characterize Pb resistant of heterotrophic bacteria in Cilalay Lake, </span><span lang="IN">West Java, </span><span>Indonesia. The water samples were collected </span><span lang="IN">along</span><span> three points around Cilalay Lake. </span><span lang="IN">Water physical and chemical </span><span>determination was performed using the Water Quality Checker</span><span lang="IN">. </span><span>The bacterial isolates were screened on T</span><span lang="IN">r</span><span>ipton</span><span lang="IN">e</span><span> Glucose Yeast (TGY) agar plates. </span><span lang="IN">Afterwards s</span><span>elected isolates were grown on Nutrient Agar media 50% </span><span lang="IN">with </span><span>supplemented Pb 100 ppm by the standard disk. Population of resistant bacteria was counted. The result from metal resistant bacteria indicated that all isolates w</span><span lang="IN">ere</span><span> resistant. The most abundant type of resistant </span><span lang="IN">bacteria </span><span>to lead was Gram negative more than Gram positive. Identified have metal resistant bacteria could be useful for the bioremediation of heavy metal contaminated sewage and waste water</span>


2019 ◽  
Vol 85 (8) ◽  
Author(s):  
Ming Peng ◽  
Xiu-Lan Chen ◽  
Dian Zhang ◽  
Xiu-Juan Wang ◽  
Ning Wang ◽  
...  

ABSTRACT The osmolyte dimethylsulfoniopropionate (DMSP) is produced in petagram quantities in marine environments and has important roles in global sulfur and carbon cycling. Many marine microorganisms catabolize DMSP via DMSP lyases, generating the climate-active gas dimethyl sulfide (DMS). DMS oxidation products participate in forming cloud condensation nuclei and, thus, may influence weather and climate. SAR11 bacteria are the most abundant marine heterotrophic bacteria; many of them contain the DMSP lyase DddK, and their dddK transcripts are relatively abundant in seawater. In a recently described catalytic mechanism for DddK, Tyr64 is predicted to act as the catalytic base initiating the β-elimination reaction of DMSP. Tyr64 was proposed to be deprotonated by coordination to the metal cofactor or its neighboring His96. To further probe this mechanism, we purified and characterized the DddK protein from Pelagibacter ubique strain HTCC1062 and determined the crystal structures of wild-type DddK and its Y64A and Y122A mutants (bearing a change of Y to A at position 64 or 122, respectively), where the Y122A mutant is complexed with DMSP. The structural and mutational analyses largely support the catalytic role of Tyr64, but not the method of its deprotonation. Our data indicate that an active water molecule in the active site of DddK plays an important role in the deprotonation of Tyr64 and that this is far more likely than coordination to the metal or His96. Sequence alignment and phylogenetic analysis suggest that the proposed catalytic mechanism of DddK has universal significance. Our results provide new mechanistic insights into DddK and enrich our understanding of DMS generation by SAR11 bacteria. IMPORTANCE The climate-active gas dimethyl sulfide (DMS) plays an important role in global sulfur cycling and atmospheric chemistry. DMS is mainly produced through the bacterial cleavage of marine dimethylsulfoniopropionate (DMSP). When released into the atmosphere from the oceans, DMS can be photochemically oxidized into DMSO or sulfate aerosols, which form cloud condensation nuclei that influence the reflectivity of clouds and, thereby, global temperature. SAR11 bacteria are the most abundant marine heterotrophic bacteria, and many of them contain DMSP lyase DddK to cleave DMSP, generating DMS. In this study, based on structural analyses and mutational assays, we revealed the catalytic mechanism of DddK, which has universal significance in SAR11 bacteria. This study provides new insights into the catalytic mechanism of DddK, leading to a better understanding of how SAR11 bacteria generate DMS.


2016 ◽  
Vol 18 (12) ◽  
pp. 4610-4627 ◽  
Author(s):  
Tristan Barbeyron ◽  
François Thomas ◽  
Valérie Barbe ◽  
Hanno Teeling ◽  
Chantal Schenowitz ◽  
...  

2012 ◽  
Vol 62 ◽  
pp. 52-60 ◽  
Author(s):  
Yendi E. Navarro-Noya ◽  
Emma Hernández-Mendoza ◽  
Jesús Morales-Jiménez ◽  
Janet Jan-Roblero ◽  
Esperanza Martínez-Romero ◽  
...  

Geobiology ◽  
2014 ◽  
Vol 12 (6) ◽  
pp. 542-556 ◽  
Author(s):  
J. Ronholm ◽  
D. Schumann ◽  
H. M. Sapers ◽  
M. Izawa ◽  
D. Applin ◽  
...  

2008 ◽  
Vol 74 (14) ◽  
pp. 4530-4534 ◽  
Author(s):  
J. Jeffrey Morris ◽  
Robin Kirkegaard ◽  
Martin J. Szul ◽  
Zackary I. Johnson ◽  
Erik R. Zinser

ABSTRACT Axenic (pure) cultures of marine unicellular cyanobacteria of the Prochlorococcus genus grow efficiently only if the inoculation concentration is large; colonies form on semisolid medium at low efficiencies. In this work, we describe a novel method for growing Prochlorococcus colonies on semisolid agar that improves the level of recovery to approximately 100%. Prochlorococcus grows robustly at low cell concentrations, in liquid or on solid medium, when cocultured with marine heterotrophic bacteria. Once the Prochlorococcus cell concentration surpasses a critical threshold, the “helper” heterotrophs can be eliminated with antibiotics to produce axenic cultures. Our preliminary evidence suggests that one mechanism by which the heterotrophs help Prochlorococcus is the reduction of oxidative stress.


1991 ◽  
Vol 6 (3) ◽  
pp. 329-340
Author(s):  
G. E. Horsnell ◽  
M. Young ◽  
J. E. Pagel ◽  
R. M. Desjardins ◽  
P. L. Seyfried

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