Mechanism of thermal aggregation of yeast alcohol dehydrogenase I

Markossian, Kira A.; Golub, Nikolay V.; Khanova, Helen A.; Levitsky, Dmitrii I.; Poliansky, Nikolay B.; Muranov, Konstantin O.; Bi, Kurganov

doi:10.1016/j.bbapap.2008.04.030

Cited by 29 publications

(23 citation statements)

References 50 publications

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“…However, and according to the classical definition of chaperones that are shown to bind only aggregation-prone proteins but not native ones (64), CP12 does not have a general chaperone activity. We show here that the protecting effect is rather specific to GAPDH, since for instance no effect of CP12 was observed on lysozyme, catalase, or alcohol dehydrogenase, proteins that are well known as chaperone substrates (31,65,66). Unlike most chaperones, CP12 forms a stable interaction with the native state of GAPDH.…”

Section: Discussionmentioning

confidence: 85%

CP12 from Chlamydomonas reinhardtii, a Permanent Specific “Chaperone-like” Protein of Glyceraldehyde-3-phosphate Dehydrogenase

Erales

Lignon

Gontero

2009

Journal of Biological Chemistry

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A new role is reported for CP12, a highly unfolded and flexible protein, mainly known for its redox function with A 4 glyceraldehyde-3-phosphate dehydrogenase (GAPDH). Both reduced and oxidized CP12 can prevent the in vitro thermal inactivation and aggregation of GAPDH from Chlamydomonas reinhardtii. This mechanism is thus not redox-dependent. The protection is specific to CP12, because other proteins, such as bovine serum albumin, thioredoxin, and a general chaperone, Hsp33, do not fully prevent denaturation of GAPDH. Furthermore, CP12 acts as a specific chaperone, since it does not protect other proteins, such as catalase, alcohol dehydrogenase, or lysozyme. The interaction between CP12 and GAPDH is necessary to prevent the aggregation and inactivation, since the mutant C66S that does not form any complex with GAPDH cannot accomplish this protection. Unlike the C66S mutant, the C23S mutant that lacks the N-terminal bridge is partially able to protect and to slow down the inactivation and aggregation. Tryptic digestion coupled to mass spectrometry confirmed that the S-loop of GAPDH is the interaction site with CP12. Thus, CP12 not only has a redox function but also behaves as a specific "chaperone-like protein" for GAPDH, although a stable and not transitory interaction is observed. This new function of CP12 may explain why it is also present in complexes involving A 2 B 2 GAPDHs that possess a regulatory C-terminal extension (GapB subunit) and therefore do not require CP12 to be redox-regulated.CP12 is a small 8.2-kDa protein present in the chloroplasts of most photosynthetic organisms, including cyanobacteria (1, 2), higher plants (3), the diatom Asterionella formosa (4, 5), and green (1) and red algae (6). It allows the formation of a supramolecular complex between phosphoribulokinase (EC 2.7.1.19) and glyceraldehyde-3-phosphate dehydrogenase (GAPDH), 3 two key enzymes of the Calvin cycle pathway, and was recently shown to interact with fructose bisphosphate aldolase, another enzyme of the Calvin cycle pathway (7). The phosphoribulokinase⅐GAPDH⅐CP12 complex has been extensively studied in Chlamydomonas reinhardtii (8, 9) and in Arabidopsis thaliana (10, 11). In the green alga C. reinhardtii, the interaction between CP12 and GAPDH is strong (8). GAPDH may exist as a homotetramer composed of four GapA subunits (A 4 ) in higher plants, cyanobacteria, and green and red algae (6, 12), but in higher plants, it can also exist as a heterotetramer (A 2 B 2 ), composed of two subunits, GapA and GapB (13,14). GapB, up to now, has exclusively been found in Streptophyta, but recently two prasinophycean green algae, Ostreococcus tauri and Ostreococcus lucimarinus, were also shown to possess a GapB gene, whereas CP12 is missing (15). The GapB subunit is similar to the GapA subunit but has a C-terminal extension containing two redox-regulated cysteine residues (16). Thus, although the A 4 GAPDHs lack these regulatory cysteine residues (13,14,(17)(18)(19)(20), they are also redox-regulated through its interaction with CP12, ...

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Section: Discussionmentioning

confidence: 85%

CP12 from Chlamydomonas reinhardtii, a Permanent Specific “Chaperone-like” Protein of Glyceraldehyde-3-phosphate Dehydrogenase

Erales

Lignon

Gontero

2009

Journal of Biological Chemistry

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“…Residues 40-60 in YADH may function as an intramolecular chaperone and prevent complete unfolding of YADH during thermal stress [34]. It has been reported that the thermal denaturation temperature T d for YADH was 63 1C, which was caused by the irreversible thermoinactivation of the protein such as thiol group oxidation, aggregation and deamidation of the protein [35]. From Fig.…”

Section: Thermal Stability Of Immobilized Yadhmentioning

confidence: 97%

Surface functionalization of chitosan-coated magnetic nanoparticles for covalent immobilization of yeast alcohol dehydrogenase from Saccharomyces cerevisiae

Zhou

et al. 2010

Journal of Magnetism and Magnetic Materials

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“…The length on the abscissa axis cut off by the linear dependence of I on R h corresponds to R h,0 value. Such an approach to the determination of the size of the start aggregates has been tested in the experiments on thermal aggregation of ␤-crystallin from calf eye lens [28,31], GAPDH [31,32] and Phb from rabbit skeletal muscle [20,31], and yeast alcohol dehydrogenase I [31,36]. When aggregation of mAAT proceeded in the absence of ␣-crystallin, R h,0 value was found to be 76 ± 3 nm (curve 1).…”

Section: Effect Of˛-crystallin On Thermal Aggregation Of Maatmentioning

confidence: 98%

Effect of α-crystallin on thermostability of mitochondrial aspartate aminotransferase

Markossian

Golub

Kleymenov

et al. 2009

International Journal of Biological Macromolecules

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Mechanism of thermal aggregation of yeast alcohol dehydrogenase I

Cited by 29 publications

References 50 publications

CP12 from Chlamydomonas reinhardtii, a Permanent Specific “Chaperone-like” Protein of Glyceraldehyde-3-phosphate Dehydrogenase

CP12 from Chlamydomonas reinhardtii, a Permanent Specific “Chaperone-like” Protein of Glyceraldehyde-3-phosphate Dehydrogenase

Surface functionalization of chitosan-coated magnetic nanoparticles for covalent immobilization of yeast alcohol dehydrogenase from Saccharomyces cerevisiae

Effect of α-crystallin on thermostability of mitochondrial aspartate aminotransferase

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