The correlation of the gene csoS2 of the carboxysome operon with two polypeptides of the carboxysome in Thiobacillus neapolitanus

1999 ◽  
Vol 172 (4) ◽  
pp. 233-239 ◽  
Author(s):  
S. H. Baker ◽  
S. C. Lorbach ◽  
M. Rodriguez-Buey ◽  
Donna S. Williams ◽  
Henry C. Aldrich ◽  
...  
Keyword(s):  
Thiobacillus Neapolitanus

The major soluble cytochromes of the obligately aerobic sulfur bacterium, Thiobacillus neapolitanus

1985 ◽  
Vol 141 (4) ◽  
pp. 273-278 ◽  
Author(s):  
P. A. Trudinger ◽  
T. E. Meyer ◽  
R. G. Bartsch ◽  
M. D. Kamen
Keyword(s):  
Thiobacillus Neapolitanus

scholarly journals Thiosulfate- and Sulfide-Dependent Pyridine Nucleotide Reduction and Gluconeogenesis in Intact Thiobacillus neapolitanus

1973 ◽  
Vol 114 (2) ◽  
pp. 592-599 ◽  
Author(s):  
Charles W. Roth ◽  
Walter P. Hempfling ◽  
Judith N. Conners ◽  
Wolf V. Vishniac
Keyword(s):  
Pyridine Nucleotide ◽  
Thiobacillus Neapolitanus

scholarly journals Energy Conservation in Thiobacillus neapolitanus C: Sulphide and Sulphite Oxidation

1977 ◽  
Vol 98 (1) ◽  
pp. 309-312 ◽  
Author(s):  
J. W. Drozd
Keyword(s):  
Energy Conservation ◽  
Thiobacillus Neapolitanus

Sequence homologs of the carboxysomal polypeptide CsoS1 of the thiobacilli are present in cyanobacteria and enteric bacteria that form carboxysomes - polyhedral bodies

1998 ◽  
Vol 76 (6) ◽  
pp. 906-916 ◽  
Author(s):  
J M Shively ◽  
C E Bradburne ◽  
H C Aldrich ◽  
T A Bobik ◽  
J L Mehlman ◽  
...  
Keyword(s):  
Klebsiella Oxytoca ◽  
Calvin Cycle ◽  
Enteric Bacteria ◽  
Bisphosphate Carboxylase ◽  
Cycle Enzyme ◽  
Synechococcus Sp ◽  
Positive Hybridization ◽  
Thiobacillus Neapolitanus ◽  
High Degree ◽  
Polyhedral Bodies

Carboxysomes containing the Calvin cycle enzyme ribulose-1,5-bisphosphate carboxylase-oxygenase (Rubisco) have been demonstrated in a variety of chemoautotrophic prokaryotes and cyanobacteria. The genes in the ccm and cso operon in Synechococcus sp. PCC7942 and Thiobacillus neapolitanus, respectively, code for several carboxysome polypeptides. The polypeptides CcmK and CsoS1 exhibit a high degree of conservation, and in turn show significant homology to the CchA and PduA polypeptides of the ethanolamine and propanediol operons of enteric bacteria. Probing Southern blots of Escherichia coli genomic DNA with csoS1A showed positive hybridization indicating the presence of a csoS1-like gene. Growing Salmonella enterica and Klebsiella oxytoca with propanediol, and E.coli with ethanolamine as the energy source under anaerobic conditions resulted in the formation of polyhedral bodies in these bacteria. The DNA - deduced amino acid sequence of three additional csoS1 genes in both Thiobacillus intermedius and Thiobacillus denitrificans was determined. The nine CsoS1 polypeptides, which includes the three previously determined for T.neapolitanus, exhibited greater than 67% sequence identity. Identity and similarity comparisons and phylogenetic analysis of known polyhedral body CsoS1-like polypeptides indicate a close structural relationship between polyhedral bodies of potentially very different function.Key words: polyhedral bodies, carboxysomes, ribulose-1,5-bisphosphate carboxylase-oxygenase, cyanobacteria, thiobacilli, enteric bacteria.

scholarly journals Regulation of Nitrogen Assimilation by the Obligate Chemolithotroph Thiobacillus neapolitanus

Microbiology ◽  
1982 ◽  
Vol 128 (1) ◽  
pp. 39-47 ◽  
Author(s):  
R. F. BEUDEKER ◽  
R. RIEGMAN ◽  
J. G. KUENEN
Keyword(s):  
Nitrogen Assimilation ◽  
Thiobacillus Neapolitanus

Electron microscopic studies of carboxysomes of Thiobacillus neapolitanus

1986 ◽  
Vol 144 (3) ◽  
pp. 258-262 ◽  
Author(s):  
Yolande A. Holthuijzen ◽  
Jan F. L. van Breemen ◽  
Wil N. Konings ◽  
Ernst F. J. van Bruggen
Keyword(s):  
Electron Microscopic ◽  
Microscopic Studies ◽  
Thiobacillus Neapolitanus

scholarly journals In situ assay of ribulose-1,5-bisphosphate carboxylase/oxygenase in Thiobacillus neapolitanus.

1991 ◽  
Vol 173 (4) ◽  
pp. 1565-1568 ◽  
Author(s):  
G C Cannon ◽  
R S English ◽  
J M Shively
Keyword(s):  
Bisphosphate Carboxylase ◽  
Thiobacillus Neapolitanus ◽  
In Situ Assay

scholarly journals Active Transport of Amino Acids by Membrane Vesicles of Thiobacillus neapolitanus

1974 ◽  
Vol 83 (2) ◽  
pp. 311-318 ◽  
Author(s):  
A. Matin ◽  
W. N. Konings ◽  
J. G. Kuenen ◽  
M. Emmens
Keyword(s):  
Amino Acids ◽  
Active Transport ◽  
Membrane Vesicles ◽  
Thiobacillus Neapolitanus

scholarly journals Insertion Mutation of the Form I cbbL Gene Encoding Ribulose Bisphosphate Carboxylase/Oxygenase (RuBisCO) in Thiobacillus neapolitanus Results in Expression of Form II RuBisCO, Loss of Carboxysomes, and an Increased CO2 Requirement for Growth

1998 ◽  
Vol 180 (16) ◽  
pp. 4133-4139 ◽  
Author(s):  
Stefanie H. Baker ◽  
Songmu Jin ◽  
Henry C. Aldrich ◽  
Gary T. Howard ◽  
Jessup M. Shively
Keyword(s):  
Immunoblot Analysis ◽  
Kanamycin Resistance ◽  
Northern Analysis ◽  
Insertion Mutation ◽  
Ribulose Bisphosphate Carboxylase ◽  
Ribulose Bisphosphate ◽  
Gene Encoding ◽  
Bisphosphate Carboxylase ◽  
Ribulose Bisphosphate Carboxylase Oxygenase ◽  
Thiobacillus Neapolitanus

ABSTRACT It has been previously established that Thiobacillus neapolitanus fixes CO2 by using a form I ribulose bisphosphate carboxylase/oxygenase (RuBisCO), that much of the enzyme is sequestered into carboxysomes, and that the genes for the enzyme, cbbL and cbbS, are part of a putative carboxysome operon. In the present study, cbbL andcbbS were cloned and sequenced. Analysis of RNA showed thatcbbL and cbbS are cotranscribed on a message approximately 2,000 nucleotides in size. The insertion of a kanamycin resistance cartridge into cbbL resulted in a premature termination of transcription; a polar mutant was generated. The mutant is able to fix CO2, but requires a CO2supplement for growth. Separation of cellular proteins from both the wild type and the mutant on sucrose gradients and subsequent analysis of the RuBisCO activity in the collected fractions showed that the mutant assimilates CO2 by using a form II RuBisCO. This was confirmed by immunoblot analysis using antibodies raised against form I and form II RuBisCOs. The mutant does not possess carboxysomes. Smaller, empty inclusions are present, but biochemical analysis indicates that if they are carboxysome related, they are not functional, i.e., do not contain RuBisCO. Northern analysis showed that some of the shell components of the carboxysome are produced, which may explain the presence of these inclusions in the mutant.

Sign in / Sign up

Export Citation Format

Share Document