The AAA+ superfamily of functionally diverse proteins

Snider, Jamie; Thibault, Guillaume; Houry, Walid

doi:10.1186/gb-2008-9-4-216

Cited by 237 publications

(200 citation statements)

References 72 publications

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“…1. These observations suggest that the Class I 46-mer has widespread distribution elsewhere in the proteome (44) and may thus have been ancestral not only to the Rossmannoid superfamily but also to other protein superfamilies. These include the enzymes characterized by Mildvan and co-workers (25)(26)(27)(28)(29) and a wider class of energy-transducing enzymes, including myosins (58), AAA ϩ motors (50,51), STAND regulators of programmed cell death (52), and signaling GTPases (59,60), all of which use P-loops to activate ATP and hence are arguably directly homologous to the Class I 46-mer. Further afield, the superfamily of metabolic enzymes in nucleotide biosynthetic pathways (53,54) may also have its origins in peptides related to the Class I 46-mer.…”

Section: Experimental Recapitulation Of Possible Assembly Of Other Momentioning

confidence: 99%

Functional Class I and II Amino Acid-activating Enzymes Can Be Coded by Opposite Strands of the Same Gene

Martínez‐Rodríguez

Erdoğan

Jimenez-Rodriguez

et al. 2015

Journal of Biological Chemistry

121

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Section: Experimental Recapitulation Of Possible Assembly Of Other Momentioning

confidence: 99%

Functional Class I and II Amino Acid-activating Enzymes Can Be Coded by Opposite Strands of the Same Gene

Martínez‐Rodríguez

Erdoğan

Jimenez-Rodriguez

et al. 2015

Journal of Biological Chemistry

121

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“…Like other AAA+ ATPases (Snider et al, 2008), Rca uses the energy from ATP hydrolysis to remodel the conformation of its target protein, Rubisco. The conformational changes induced by Rca restore catalytic competence to Rubisco active sites that have been inactivated by the unproductive binding of sugar phosphates, including the substrate ribulose 1,5-bisphosphate (RuBP; Wang and Portis, 1992).…”

mentioning

confidence: 99%

The Regulatory Properties of Rubisco Activase Differ among Species and Affect Photosynthetic Induction during Light Transitions

2013

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Rubisco's catalytic chaperone, Rubisco activase (Rca), uses the energy from ATP hydrolysis to restore catalytic competence to Rubisco. In Arabidopsis (Arabidopsis thaliana), inhibition of Rca activity by ADP is fine tuned by redox regulation of the a-isoform. To elucidate the mechanism for Rca regulation in species containing only the redox-insensitive b-isoform, the response of activity to ADP was characterized for different Rca forms. When assayed in leaf extracts, Rubisco activation was significantly inhibited by physiological ratios of ADP to ATP in species containing both a-Rca and b-Rca (Arabidopsis and camelina [Camelina sativa]) or just the b-Rca (tobacco [Nicotiana tabacum]). However, Rca activity was insensitive to ADP inhibition in an Arabidopsis transformant, rwt43, which expresses only Arabidopsis b-Rca, although not in a transformant of Arabidopsis that expresses a tobacco-like b-Rca. ATP hydrolysis by recombinant Arabidopsis b-Rca was much less sensitive to inhibition by ADP than recombinant tobacco b-Rca. Mutation of 17 amino acids in the tobacco b-Rca to the corresponding Arabidopsis residues reduced ADP sensitivity. In planta, Rubisco deactivated at low irradiance except in the Arabidopsis rwt43 transformant containing an ADP-insensitive Rca. Induction of CO 2 assimilation after transition from low to high irradiance was much more rapid in the rwt43 transformant compared with plants containing ADP-sensitive Rca forms. The faster rate of photosynthetic induction and a greater enhancement of growth under a fluctuating light regime by the rwt43 transformant compared with wild-type Arabidopsis suggests that manipulation of Rca regulation might provide a strategy for enhancing photosynthetic performance in certain variable light environments.

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“…A range of MS conditions was tested (e.g., different cone voltages), and the current conditions were those under which spectra could be obtained at sufficient signal-to-noise, where the peak width was not too broad and where the highest oligomeric forms were maintained. Nevertheless, while the prior biochemical methods were unable to ascribe a definitive stoichiometry for a fully assembled RA oligomer, the nanoESI-MS data indicate tobacco RA can form hexamers, the common subunit conformation shared by most AAA+proteins [38,39].…”

Section: Molecular Mass Of Rubisco Activase (Ra)mentioning

confidence: 99%

NanoESI Mass Spectrometry of Rubisco and Rubisco Activase Structures and Their Interactions with Nucleotides and Sugar Phosphates

Blayney

Whitney

Beck

2011

J. Am. Soc. Mass Spectrom.

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Ribulose bisphosphate carboxylase/oxygenase (Rubisco) is the protein that is responsible for the fixation of carbon dioxide in photosynthesis. Inhibitory sugar phosphate molecules, which can include its substrate ribulose-1,5-bisphosphate (RuBP), can bind to Rubisco catalytic sites and inhibit catalysis. These are removed by interaction with Rubisco activase (RA) via an ATP hydrolytic reaction. Here we show the first nanoESI mass spectra of the hexadecameric Rubisco and of RA from a higher plant (tobacco). The spectra of recombinant, purified RA revealed polydispersity in its oligomeric forms (up to hexamer) and that ADP was bound. ADP was removed by dialysis against a high ionic strength solution and nucleotide binding experiments showed that ADP bound more tightly to RA than AMP-PNP (a non-hydrolysable ATP analog). There was evidence that there may be two nucleotide binding sites per RA monomer. The oligomerization capacity of mutant and wild-type tobacco RA up to hexamers is analogous to the subunit stoichiometry for other AAA+ enzymes. This suggests assembly of RA into hexamers is likely the most active conformation for removing inhibitory sugar phosphate molecules from Rubisco to enable its catalytic competency. Stoichiometric binding of RuBP or carboxyarabinitol bisphosphate (CABP) to each of the eight catalytic sites of Rubisco was observed.

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The AAA+ superfamily of functionally diverse proteins

Abstract: The AAA+ superfamily is a large superfamily of ATPases that are characterized by a conserved catalytic module, the AAA+ module. Members are involved in an astonishing range of different cellular processes.

Cited by 237 publications

References 72 publications

Functional Class I and II Amino Acid-activating Enzymes Can Be Coded by Opposite Strands of the Same Gene

Functional Class I and II Amino Acid-activating Enzymes Can Be Coded by Opposite Strands of the Same Gene

The Regulatory Properties of Rubisco Activase Differ among Species and Affect Photosynthetic Induction during Light Transitions

NanoESI Mass Spectrometry of Rubisco and Rubisco Activase Structures and Their Interactions with Nucleotides and Sugar Phosphates

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