Adenine Nucleotide-mediated Subunit Exchange between Isoenzymes of Glyceraldehyde-3-phosphate Dehydrogenase

Lebherz, Herbert G.; Savage, B; Abächerli, Erika

doi:10.1038/newbio245269a0

Cited by 23 publications

(6 citation statements)

References 15 publications

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“…andD D (FROSCH et al 1973, FROSCH andWAGNER 1973a). This conception is supported by i n v i t r o studies on trout NAD-GPD which demonstrated ATP mediated, and pyridine nucleotide inhibited, exchange in subunits of GPD-tetrameres in the synthesis of GPD-isozymes (LEBHERZ et al 1973).…”

Section: Discussionmentioning

confidence: 91%

“…In view of the increasing evidence for nucleotide control of the specificity and activity of triosephosphate dehydrogenases (PUPILLO and PICCARI 1973, MULLER 1970, MULLER et al 1969, YANG and DEAL 1969a, b, LEBHERZ et al 1973, PAWLIZKI and LATZKO 1974, the time courses of the pool size levels in adenine-and pyridine nucleotides were of great importance. The kinetics of the pyridine nucleotides ( fig.…”

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Endogenous rhythmicity and energy transductionv. rhythmicity in adenine nucleotides and energy charge in seedlings of Chenopodium rubrum∗∗

Wagner

Stroebele

Frosch

1974

Journal of Interdisciplinary Cycle Research

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Section: Discussionmentioning

confidence: 91%

Section: Discussionmentioning

confidence: 99%

Endogenous rhythmicity and energy transductionv. rhythmicity in adenine nucleotides and energy charge in seedlings of Chenopodium rubrum∗∗

Wagner

Stroebele

Frosch

1974

Journal of Interdisciplinary Cycle Research

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“…Interestingly, NAD + prevents hybridization, suggesting that it helps stabilize the GAPDH tetramer. Lebherz and coworkers [136] demonstrated ATP-induced hybridization, which was also inhibited by NAD + as well as NADH. Small amounts of SR 3 and S 3 R (where, S is succinylated subunit) were observed at high ionic strength [75], suggesting the appearance of monomers.…”

Section: Tetrameric Hybridsmentioning

confidence: 97%

Dynamic Oligomeric Properties

Seidler

2012

GAPDH: Biological Properties and Diversity

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This chapter provides a foundation for further research into the relationship between dynamic oligomeric properties and functional diversity. The structural basis that underlies the conformational sub-states of the GAPDH oligomer is discussed. The issue of protein stability is given a thorough analysis, since it is well-established that the primary strategy for protein oligomerization is to stabilize conformation. Several factors that affect oligomerization are described, including chemical modification by synthetic reagents. The effects of native substrates and coenzymes are also discussed. The curious feature of chloride ions having a de-stabilizing effect on native GAPDH structure is described. Additionally, the role of adenine dinucleotides in tetramer-dimer equilibrium dynamics is suggested to be a major part of the physiological regulation of GAPDH structure and function. This chapter also contends that a vast amount of useful information can come from comparative analyses of diverse species, particularly regarding protein stability and subunit-subunit interaction. Lastly, the concept of domain exchange is introduced as a means of understanding the stabilization of dynamic oligomers, suggesting that inter-subunit contacts may also be a way of masking docking sites to other proteins.

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“…The amino acid sequences of the lobster (Davidson et al, 1967), rabbit (J. I. Harris, personal communication) and yeast (Jones & Harris, 1972) glyceraldehyde 3-phosphate dehydrogenases are closely homologous. Also it is possible to form molecular hybrids between glyceraldehyde 3-phosphate dehydrogenase molecules from a wide variety of species (Chilson et al, 1966;Spotorno & Hollaway, 1970;Lebherz et al, 1973;Kochman et al, 1974). Therefore it seems likely that the three-dimensional molecular structures of these enzymes are similar.…”

Section: Discussionmentioning

confidence: 99%

The investigation of substrate-induced changes in subunit interactions in glyceraldehyde 3-phosphate dehydrogenases by measurement of the kinetics and thermodynamics of subunit exchange

Osborne¹,

Hollaway²

1975

Biochemical Journal

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An investigation was made of changes in subunit interactions in glyceraldehyde 3-phosphate dehydrogenase on binding NAD+, NADH and other substrates by using the previously developed method of measurement of rates and extent of subunit exchange between the rabbit enzyme (R4), yeast enzyme (Y4) and rabbit-yeast hybrid (R2Y2) [Osborne & Hollaway (1974) Biochem. J. 143, 651-662]. The free energy of activation for the conversion of tetramer into dimer for the rabbit enzyme (R4 leads to 2R2) is increased by at least 12kJ/mol in the presence of NAD+. This increase is interpreted in terms of an NAD+-induced 'tightening' of the tetrameric structure probably involving increased interaction at the subunit interfaces across the QR plane of the molecule [see Buehner et al. (1974) J. Mol. Biol. 82, 563-585]. This tightening of the structure only occurs on binding the third NAD+ molecule to a given enzyme molecule. Conversely, binding of NADH causes a decrease in the free energy of activation for the R4 leads to 2R2 and Y4 leads to 2Y2 conversions by at least 10kJ/mol. This is interpreted as a NADH-induced 'loosening' of the structures arising from decreased interactions across the subunit interfaces involving the QR dissociation plane. In the presence of NADH the increase in the rate of subunit exchange is such that it is not possible to separate the hybrid from the other species if electrophoresis is carried out with NADH in the separation media. In the presence of a mixture of NADH and NAD+ the effect of NAD+ on subunit exchange is dominant. The results are discussed in terms of the known co-operativty between binding sites in glyceraldehyde 3-phosphate dehydrogenases.

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Adenine Nucleotide-mediated Subunit Exchange between Isoenzymes of Glyceraldehyde-3-phosphate Dehydrogenase

Cited by 23 publications

References 15 publications

Endogenous rhythmicity and energy transductionv. rhythmicity in adenine nucleotides and energy charge in seedlings of Chenopodium rubrum∗∗

Endogenous rhythmicity and energy transductionv. rhythmicity in adenine nucleotides and energy charge in seedlings of Chenopodium rubrum∗∗

Dynamic Oligomeric Properties

The investigation of substrate-induced changes in subunit interactions in glyceraldehyde 3-phosphate dehydrogenases by measurement of the kinetics and thermodynamics of subunit exchange

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