Progr Phycol Res 4: — Curr Genet — Anal Biochem 6—13 PubMed Google Scholar. J Mol Biol — J Phycol — Mol Gen Genet — Nucleic Acids Res — Ann Rev Biochem — Article PubMed Google Scholar.
Nierzwicki-Bauer SA, Curtis Se, Haselkorn R: Cotranscription of genes encoding the small and large subunits of ribulose-1,5-bisphosphate carboxylase in the cyanobacterium Anabaena Reith M, Cattolico RA: Inverted repeat of Olisthodiscvs luteus chloroplast DNA contains genes for both subunits of ribulose-1,5-bisphosphate carboxylase and the dalton QB protein: phylogenetic implications.
Plant Mol Biol 7: — Shinozaki K, Sugiura M: The gene for the small subunit of ribulose-1,5-bisphosphate is located close to the gene for the large subunit in the cyanobacterium Anacystis nidulans Planta Berl — All other hydrophobic residues that surround Ser forming the pocket are coloured red. Further investigation into the above localized structural change led us to another amino acid, Ser, which was predicted to have similar effects on oxygen sensitivity of the A.
Ser is situated in what appears to be a hydrophobic pocket that surrounds one side of the active site Fig. In addition, the model structure shows an interaction of the side chain of Ser with two highly conserved and catalytically important residues, Gly and Thr Gly and Thr, found in all forms of Rubisco, show no interactions with the amino acid residue equivalent to Ser of RbcL2 in form I and form II enzymes.
Thus, this unique interaction and positioning of Ser in a key hydrophobic pocket of RbcL2, similar to Met, suggested that Ser of RbcL2 might be a likely candidate for further investigation by site-directed mutagenesis.
Ser was thus changed to residues found in equivalent positions in form I and form II enzymes alanine and isoleucine, respectively, and valine. Clearly, the above studies point to the importance of hydrophobic regions for interactions with oxygen, with the oxygen-sensitive A. Prokaryotic bioselection after random mutagenesis has now become feasible and adapted for the isolation of mutant forms of Rubisco Smith and Tabita, ; Green et al.
It is convenient to use Rhodobacter capsulatus , with its endogenous form I and form II Rubisco genes deleted, as a host strain for whatever prokaryotic Rubisco we wish to study Finn and Tabita, ; Smith and Tabita, , Both R.
Recovery of mutants is also made simple by the fact that CO 2 fixation is dispensable in these organisms and strains may be grown under aerobic heterotrophic conditions as with Escherichia coli.
Clearly, growth at various levels and ratios of CO 2 and O 2 provides intriguing selective pressures to isolate potentially useful mutant forms of Rubisco, in an intracellular environment where Rubisco normally functions.
This system thus far appears inherently more stable than artificial systems recently developed Parikh et al. Moreover, the R.
As illustrated for cyanobacterial Rubisco Fig. Thus, specific alterations on each subunit may be assessed after normal protein assembly in E. To ensure constant levels of expression, the rbcLrbcS genes are under the control of the transcriptional regulator CbbR and the cbbM promoter from R.
The two plasmids are resistant to different antibiotics and belong to two different incompatability groups. Both plasmids can be co-expressed in the Rubisco-deficient strain of R.
Several interesting mutant cyanobacterial Synechococcus sp. Of particular interest were residues that were distal to the active site that were localized at monomer—monomer or dimer—dimer interfaces and appeared to influence important kinetic constants, particularly the K c.
One of these mutant proteins, DV, was shown not to be able to support growth in R. Asp is localized on the surface of one monomer of a dimeric pair, where it contacts Ser of a monomer from a second dimeric pair of large subunits.
To gain an understanding as to how Asp, which is far from the active site, might influence catalysis, an attempt was made to isolate specific internal suppressor mutations which, it was surmised, would overcome the effect of DV, provide insights into residues that might interact with Asp, and subsequently allow growth in the R. Over several years, multiple investigators in our laboratory were all able to isolate a single suppressor mutation that allowed growth in the R.
This suppressor or compensatory protein, a DVAV double mutant, was found to possess an improved K c. Furthermore, it appears that both Asp and Ala exert their influence on Ser, an important active-site residue required for binding the P2 phosphate of the substrate ribulose 1,5 -bis phospate S Satagopan et al. Most importantly, however, Ala was subsequently shown to be localized in an interesting hydrophobic region near the active site.
The adjacent residue, which is an active-site Ser is coloured in all the three structures. The active-site ligands, i. Why might this hydrophobic region be important? As discussed above, Ser of the archaeal A. Further studies with the equivalent Ala residue of form I Rubisco have also recently shown that this residue influences the ability of the cyanobacterial enzyme to support aerobic chemolithoautotrophic growth in the R.
Moreover, as expected, this residue also directly affects the K o value S Satagopan et al. It is apparent that Rubisco, and its homologue, the Rubisco-like protein, share an interesting history and undoubtedly present a classic example of divergent evolution. The different forms of Rubisco found in nature, some of which must function in very extreme or inhospitable environments, almost by definition, have made structural adaptations to allow catalysis to occur.
Investigating these structural adaptations is very useful, as such studies provide a framework for understanding more about Rubisco structure and function in general. Google Scholar. Google Preview. Oxford University Press is a department of the University of Oxford. It furthers the University's objective of excellence in research, scholarship, and education by publishing worldwide.
Sign In or Create an Account. Sign In. Advanced Search. Search Menu. Article Navigation. Close mobile search navigation Article Navigation. Volume Biochemistry 23 , — Styring, S. Biochemistry 24 , — Schloss, J. Biochemistry 27 , — Estelle, M. Robison, P. Biochemistry 18 , — Hartman, F. Herndon, C. Biochemistry 21 , — Larimer, F. Kabsch, W. FEBS Lett. Download references. Central Research and Development Department, E. You can also search for this author in PubMed Google Scholar.
Reprints and Permissions. Crystal structure of the active site of ribulose-bisphosphate carboxylase. Download citation. Biogenesis and metabolic maintenance of Rubisco. Plant Biol. Brutnell, T. Plant Cell 11, — Cloney, L. Assessment of plant chaperonin gene function in Escherichia coli. Expression of plant chaperonin genes in Escherichia coli. Dereeper, A. BMC Evol. Nucleic Acids Res. Dickson, R. Reconstitution of higher plant chloroplast chaperonin 60 tetradecamers active in protein folding.
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