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Ohio Plant Biotechnology Consortium

Member Institutions:

Robert Tabita

Professor
Department of Microbiology
Department of Natural Resources
The Ohio State University
Room 363 Botany and Zoology Building
1735 Neil Avenue
Columbus, Ohio 43210
Phone: Office (614) 292-1982, Lab (614) 292-9371
email tabita.1@osu.edu

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Robert Tabita

Research Interests

My laboratory is concerned with the molecular regulation, biochemistry, and enzymology of carbon dioxide assimilation. All organisms require CO2 and many enzyme-catalyzed reactions employ CO2 as a reactant for processes as important and varied as carbohydrate metabolism, lipid biosynthesis, and the production of important metabolic intermediates for the cell. With the realization that many microorganisms require CO2 in order to elicit pathogenesis, it is not surprising that CO2 metabolism and its control has great health relevance. Carbon dioxide may also be employed as the sole source of carbon by a large and diverse group of organisms on this planet. For this reason, CO2 fixation is a process that is associated with global issues of agricultural productivity, carbon cycling, and industrial productivity. CO2 is also recognized as the chief “green house” gas and has been implicated in the general warming of the earth’s biosphere. For all these reasons, research on various aspects of CO2 fixation control, biochemistry, and ecology have attracted wide interest.

Selected References

Molecular Regulation of CO2 Fixation

  • Gibson, J.L., Falcone, D.L., and F.R. Tabita.  Nucleotide sequence, transcriptional analysis, and expression of genes encoded within the form I CO2
  • fixation operon of Rhodobacter sphaeroides.  J. Biol.Chem. 266 (1991) 14646-14653.
  • Falcone, D.L., and Tabita, F.R.  Complementation analysis and regulation of CO2
  • fixation gene expression in a ribulose 1,5-bisphosphate carboxylase-oxygenase deletion strain of Rhodospirillum rubrum.  J. Bacteriol. 175 (1993) 5066-5077.
  • Gibson, J.L., and Tabita, F.R.  Nucleotide sequence and functional analysis of CbbR, a positive regulator of the Calvin cycle operons of Rhodobacter sphaeroides.  J. Bacteriol. 175 (1993) 5778-5784.
  • Xu, H.H., and Tabita, F.R.  Positive and negative regulation of sequences upstream of the form II cbb CO2
  • fixation operon of Rhodobacter sphaeroides.  J. Bacteriol. 176 (1994) 7299-7308. 
  • Tabita, F.R.  The biochemistry and metabolic regulation of carbon metabolism and CO2
  • fixation in purple bacteria.  In, Anoxygenic Photosynthetic Bacteria (R.E. Blankenship, M.T. Madigan, and C.E. Bauer, eds.) Kluwer Acad. Publ. (1995) (pp. 885-914).
  • Qian, Y., and Tabita, F.R.  A global signal transduction system regulates aerobic and anaerobic CO2
  • fixation in Rhodobacter sphaeroides. J. Bacteriol. 178 (1996) 12-18.
  • Gibson, J.L., and Tabita, F.R.  The molecular regulation of the reductive pentose phosphate pathway in proteobacteria and cyanobacteria (minireview).  Arch. Microbiol. 166 (1996) 141-150.
  • Joshi, H.M., and Tabita, F.R.  A global two component signal transduction system that integrates the control of photosynthesis, carbon dioxide assimilation, and nitrogen fixation. Proc. Natl. Acad. Sci. USA 93 (1996) 14515-14520.
  • Gibson, J.L., and Tabita, F.R.  Analysis of the cbbXYZ operon in Rhodobacter sphaeroides.  J. Bacteriol. 179 (1997) 663-669.
  • Paoli, G.C., Vichivanives, P., and Tabita, F.R.  Physiological control and cbb gene  regulation in Rhodobacter capsulatus. J. Bacteriol. 180 (1998) 4258-4269. 
  • Qian, Y., and Tabita, F.R.  Expression of glnB and a glnB-like gene in a ribulose bisphosphate carboxylase/oxygenase (RubisCO) deletion mutant of Rhodobacter sphaeroides J. Bacteriol.  180 (1998) 4644-4649.
  • Dubbs, J.M., and Tabita, F.R.  Two functionally distinct regions upstream of the cbbI operon of Rhodobacter sphaeroides regulate gene expression.  J. Bacteriol.  180 (1998) 4093-4911

Enzymology and Biochemistry of CO2 Fixation

  • Read, B.A., and F.R. Tabita.  Amino acid substitutions in the small  subunit of ribulose 1,5 bisphosphate carboxylase/oxygenase that influence catalytic activity of the holoenzyme.  Biochemistry.  31 (1992) 519-525.
  • Read, B.A., and Tabita, F.R.  A hybrid ribulose bisphosphate carboxylase/oxygenase enzyme exhibiting a substantial increase in substrate specificity factor.  Biochemistry 31 (1992) 5553-5560.
  • Li, L.-A., Gibson, J.L., and Tabita, F.R.  The RubisCO activase (rca) gene is located downstream from rbcS in Anabaena sp. strain CA and is detected in other Nostoc/Anabaena strains.  Plant Mol. Biol. 21 (1993), 753-764.
  • Tabita, F.R.  The biochemistry and molecular regulation of carbon dioxide metabolism in cyanobacteria.  In, The Molecular Biology of the cyanobacteria (D.A. Bryant, ed.) Kluwer Acad. Pub. (1994), pp. 299-329.
  • Read, B.A., and Tabita, F.R.  High substrate specificity factor ribulose bisphosphate 
    carboxylase/oxygenase from eukaryotic marine algal and properties of recombinant cyanobacterial rubisco containing "algal" residue modifications.  Arch. Biochem. Biophys. 312 (1994) (210-218).
  • Li, L.-A., and Tabita, F.R.  Transcription control of ribulose bisphosphate carboxylase/oxygenase activase and adjacent genes in Anabaena species.  J.Bacteriol.  176 (1994) 6697-6706.
  • Hernandez, J.M., Baker, S.H., Lorbach, S.C., Shively, J.M., and Tabita, F.R.  Deduced amino acid  sequence, functional expression, and unique enzymatic properties of form I and form II ribulose bisphosphate carboxylase/oxygenase from the chemoautotrophic bacteriun Thiobacillus denitrificans.  J. Bacteriol. 178 (1996) 347-356.
  • Wahlund, T.E., and Tabita, F.R.  The reductive tricarboxylic and cycle of carbon dioxide assimilation: initial studies and purification of ATP-citrate lyase from the green sulfur bacterium Chlorobium tepidum.  J. Bacteriol. 179 (1997) 4859-4867.
  • Li, L.-A., and Tabita, F.R.  Maximum activity of recombinant ribulose 1,5-bisphosphate carboxylase/oxygenase of Anabanea sp. strain CA requires the product of the rbcX gene.  J. Bacteriol. 179 (1997) 3793-3796.
  • Watson, G.M.F., and Tabita, F.R.  Microbial ribulose 1,5-bisphosphate carboxylase/oxygenase: a molecule for phylogenetic and enzymological investigation.  FEMS Microbiol. Lett. 146 (1997) 13-22.
  • Ramage, R.T., Read, B.A., and Tabita, F.R.  Alteration of the alpha helix region of cyanobacterial ribulose 1,5-bisphosphate carboxylase/oxygenase to reflect sequences found in high substrate specificity enzymes.  Arch. Biochem. Biophys. 348  (1998) 81-88.
  • Lee, W.T., G.M.F. Watson, and F.R. Tabita.  Chaperonins of the purple nonsulfur bacterium Rhodobacter sphaeroides.  Meth. Enzymol154-161. 290 (1998).
  • Horken, K.M., and Tabita, F.R. Closely related form I ribulose bisphosphate carboxylase/oxygenase molecules that possess different CO2
  • /O2 substrate specificities. Arch. Biochem. Biophys. 361 (1999) 183-194.
  • Novak, J.S., and Tabita, F.R. Molecular approaches to probe differential NADH activation of  phosphoribulokinase isozyes from Rhodobacter sphaeroides. Arch. Biochem. Biophys. 363 (1999)273-282
  • Watson, G.M.F., Yu, J.-P., Yu, and Tabita, F.R. Unusual ribulose 1,5- bisphosphate carboxylase/oxygenase of anoxic Archaea. J. Bacteriol. 181 (1999) 1569-1575.
  • Li, l.-A., Zianni, M.R., and Tabita, F.R. Inactivation of the monocistronic rca gene in Anabaena variabilis suggests a physiological ribulose bisphosphate carboxylase/oxygenase activase – like function in heterocystous cyanobateria. Plant Mol. Biol. (in press).
  • Tabita, F.R. Microbial ribulose bisphosphate carboxylase/oxygenase: a different perspective. Invited review. Photosynthesis Research (in press).

Molecular Ecology of CO2 Fixation

  • Pichard, S.L., Brown, J.B., Campbell, L., Tabita, F.R., and Paul, J.H.  Regulation of ribulose bisphosphate carboxylase in natural phytoplankton communities.  I. Diel rhythyms.  Mar. Ecol. Prog. Ser. 139 (1996) 257-265.
  • Watson, G.M.F., and Tabita, F.R.  Regulation, unique gene organization, and unusual primary structure of carbon fixation genes from a marine phycoerythrin-containing cyanobacterium.  Plant Mol. Biol. 32 (1996) 1103-1115.
  • Xu, H.H., and Tabita, F.R.  Ribulose-1,5-bisphosphate carboxylase/oxygenase gene expression and diversity of Lake Erie planktonic microorganisms.  Appl. and Env. Microbiol. 62 (1996) 1913-1921.
  • Pichard, S.L., Campbell, L., Carder, K., Kang, J.B., Tabita, F.R., and  Paul, J.H.  Analysis of ribulose bisphosphate carboxylase gene expression in natural phytoplankton communities by group-specific gene probing.  Mar. Ecol. Prog. Ser. 149 (1997) 239-253.
  • Paul, J.S., Pichard, S.L., Kang, J.B., Watson, G.M.F., and Tabita, F.R. Evidence for a clade-specific temporal and spatial separation in ribulose bisphosphate carboxylase gene expression in phytoplankton populations off Cape Hatteras and Bermuda. Limnol. Oceanogr. 44 (1999) 12-23.

Applied Studies

  • Wahlund, T.M., Conway, T., and Tabita, F.R.  Bioconversion of CO2 to ethanol and other compounds. Symp. on the Capture, Utilization and Disposal of CO2, Amer. Chem. Soc. Div. Fuel. Chem. 41 (1996) 1403-1406.

Dr. Tabita's Faculty Summary
Ohio State Department of Microbiology
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