scholarly journals Comparative Genomics of Beggiatoa leptomitoformis Strains D-401 and D-402T with Contrasting Physiology But Extremely High Level of Genomic Identity

2020 ◽  
Vol 8 (6) ◽  
pp. 928
Author(s):  
Tatyana S. Rudenko ◽  
Sergey V. Tarlachkov ◽  
Nikolay D. Shatskiy ◽  
Margarita Yu. Grabovich

Representatives of filamentous colorless sulfur-oxidizing bacteria often dominate in sulfide biotopes, preventing the diffusion of toxic sulfide into the water column. One of the most intriguing groups is a recently described Beggiatoa leptomitoformis including strains D-401 and D-402T. Both strains have identical genes encoding enzymes which are involved in the oxidation of hydrogen sulfide and thiosulfate. Surprisingly, the B. leptomitoformis strain D-401 is not capable to grow lithotrophically in the presence of reduced sulfur compounds and to accumulate elemental sulfur inside the cells, in contrast to the D-402T strain. In general, genomes of D-401 and D-402T have an extremely high level of identity and only differ in 1 single-letter substitution, 4 single-letter indels, and 16 long inserts. Among long inserts, 14 are transposons. It was shown that in the D-401 strain, a gene coding for a sulfur globule protein was disrupted by one of the mentioned transposons. Based on comparative genomics, RT-qPCR, and HPLC-MS/MS, we can conclude that this gene plays a crucial role in the formation of the sulfur globules inside the cells, and the disruption of its function prevents lithotrophic growth of B. leptomitoformis in the presence of reduced sulfur compounds.

Microbiology ◽  
2010 ◽  
Vol 156 (3) ◽  
pp. 764-773 ◽  
Author(s):  
Frauke Grimm ◽  
Nadine Dobler ◽  
Christiane Dahl

Sulfur globules are formed as obligatory intermediates during the oxidation of reduced sulfur compounds in many environmentally important photo- and chemolithoautotrophic bacteria. It is well established that the so-called Dsr proteins are essential for the oxidation of zero-valent sulfur accumulated in the globules; however, hardly anything is known about the regulation of dsr gene expression. Here, we present a closer look at the regulation of the dsr genes in the phototrophic sulfur bacterium Allochromatium vinosum. The dsr genes are expressed in a reduced sulfur compound-dependent manner and neither sulfite, the product of the reverse-acting dissimilatory sulfite reductase DsrAB, nor the alternative electron donor malate inhibit the gene expression. Moreover, we show the oxidation of sulfur to sulfite to be the rate-limiting step in the oxidation of sulfur to sulfate as sulfate production starts concomitantly with the upregulation of the expression of the dsr genes. Real-time RT-PCR experiments suggest that the genes dsrC and dsrS are additionally expressed from secondary internal promoters, pointing to a special function of the encoded proteins. Earlier structural analyses indicated the presence of a helix–turn–helix (HTH)-like motif in DsrC. We therefore assessed the DNA-binding capability of the protein and provide evidence for a possible regulatory function of DsrC.


1981 ◽  
Vol 8 (1-2) ◽  
pp. 71-88 ◽  
Author(s):  
Martin F. Tansy ◽  
Frank M. Kendall ◽  
John Fantasia ◽  
Wendell E. Landin ◽  
Richard Oberly ◽  
...  

2021 ◽  
pp. 118504
Author(s):  
Paul Van Rooy ◽  
Ryan Drover ◽  
Tanner Cress ◽  
Cara Michael ◽  
Kathleen L. Purvis-Roberts ◽  
...  

1981 ◽  
Vol 147 (1) ◽  
pp. 140-154 ◽  
Author(s):  
D C Nelson ◽  
R W Castenholz

1988 ◽  
Vol 150 (6) ◽  
pp. 574-579 ◽  
Author(s):  
W. Hazeu ◽  
W. H. Batenburg-van der Vegte ◽  
P. Bos ◽  
R. K. van der Pas ◽  
J. G. Kuenen

1983 ◽  
Vol 55 (1) ◽  
pp. 135-138 ◽  
Author(s):  
Thomas J. Kelly ◽  
Jeffrey S. Gaffney ◽  
Mary F. Phillips ◽  
Roger L. Tanner

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