Phosphorus-31 nuclear magnetic resonance studies of adenosine 5'-triphosphate bound to a nitrated derivative of G-actin

Brauer, Manfred; Sykes, Brian D.

doi:10.1021/bi00527a005

Cited by 35 publications

(37 citation statements)

References 36 publications

(56 reference statements)

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“…A variety of techniques have been used to approach this problem: a nuclear magnetic resonance (NMR) study suggested the cation and nucleotide sites were separated by no more than 10 ~ (Brauer & Sykes, 1982), and fluorescence resonance energy transfer (FRET) measurements (Miki & Wahl, 1985) supported this distance of separation. On the other hand, other groups using proton NMR, fluorescence spectroscopy and FRET techniques concluded the cation and nucleotide binding sites are separated by 16 ,k (Barden & dos Remedios, 1984Hambly et al, 1986;dos Remedios et al, 1987).…”

Section: Localization Of Tightly-bound Cation and Nucleotide Binding mentioning

confidence: 99%

Tightly-bound divalent cation of actin

Estes

Selden

Kinosian

et al. 1992

J Muscle Res Cell Motil

134

135

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Actin is known to undergo reversible monomer-polymer transitions that coincide with various cell activities such as cell shape changes, locomotion, endocytosis and exocytosis. This dynamic state of actin filament self-assembly and disassembly is thought to be regulated by the properties of the monomeric actin molecule and in vivo by the influence of actin-associated proteins. Of major importance to the properties of the monomeric actin molecule are the presence of one tightly-bound ATP and one tightly-bound divalent cation per molecule. In vivo the divalent cation is thought to be Mg2+ (Mg-actin) but in vitro standard purification procedures result in the preparation of Ca-actin. The affinity of actin for a divalent cation at the tight binding site is in the nanomolar range, much higher than earlier thought. The binding kinetics of Mg2+ and Ca2+ at the high affinity site on actin are considered in terms of a simple competitive binding mechanism. This model adequately describes the published observations regarding divalent cation exchange on actin. The effects of the tightly-bound cation, Mg2+ or Ca2+, on nucleotide binding and exchange on actin, actin ATP hydrolysis activity and nucleation and polymerization of actin are discussed. From the characteristics that are reviewed, it is apparent that the nature of the bound divalent cation has a significant effect on the properties of actin.

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Section: Localization Of Tightly-bound Cation and Nucleotide Binding mentioning

confidence: 99%

Tightly-bound divalent cation of actin

Estes

Selden

Kinosian

et al. 1992

J Muscle Res Cell Motil

134

135

View full text Add to dashboard Cite

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“…However, this conclusion is controversial and others using FRET (Miki & Wahl, 1985), NMR (Brauer & Sykes, 1981, 1982 and EPR (Loscalzo & Reed, 1976) reported that the Me and nudeotide bind to actin as a complex. Still others (Nowak et al, 1988) have proposed that the metal and nucleotide may bind as a complex and that subsequently their positions are rearranged.…”

Section: High Affinity Metal Binding Site (Me)mentioning

confidence: 99%

Structure of actin observed by fluorescence resonance energy transfer spectroscopy

Miki

O’Donoghue

1992

J Muscle Res Cell Motil

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“…These two mechanisms are called chemical shift anisotropy and dipole-dipole interactions. In the limit of large, slow-tumbling macromolecules and no internal motion of the nuclei on the ligand, the sum of these two contributions to the spin-spin and spin-lattice relaxation rates are (5) where y~ and yp are the gyromagnetic ratios of the proton and phosphorus nuclei, respectively; r~~ is the internuclear proton-phosphorus distance; wp is the phosphorus resonance frequency (in radians per second); a, is the rotational correlation time of the phos- respectively. Further, the two unknowns for each mechanism (chemical shift anisotropy factor (Aa)(l + q2/3)1'2 and correlation time 7, for chemical shift anisotropy or internuclear distance r~~ and correlation time 7, for dipole-dipole) can be separated once the contributions of the two mechanisms to 1 /T2 and 1 /TI are known.…”

Section: Theory Of Nmwmentioning

confidence: 99%

“…While the work on myosin was underway, Fred Brauer began to look at actin (5,25). Actin is the major component of the thin filament of muscle, is intimately involved in the contractile cycle, and is ubiquitous in muscle and nonmuscle cells as a structural element.…”

Section: Actinmentioning

confidence: 99%

Applications of ³¹P nuclear magnetic resonance to studies of protein structure and function

Sykes¹

1983

Can. J. Biochem. Cell Biol.

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Sykes, B. B. (1983) Applications of 3 '~ nuclear magnetic resonance to studies of protein structure and function. Can. J.Biochem. Cell Biol. 51, 155-1 6 4 Selective illustrative applications of phosphorus-3 1 nuclear magnetic resonance spectroscopy to the study of protein structure and function are reviewed, including the enzymes alkaline phosphatase, myosin, actin, and glycogen phosphorylase. Svkes, B. B. (1983) Applications of 3 '~ nuclear magnetic resonance to studies of protein structure and function. Can. J. Biochem. Cell Biol. 51, 155-1 6 4Revue des applications de la spectrsscopie de resonance magnktique nuclkaire du phosphore-31 B l'ktude de la structure et des fonction des proteines incluant les enzymes suivant: phosphatase alcaline, myosine, actine et glycogkne phosphorylase.[Traduit par la revue]?his statement refers to commonly used spin 1 /2 nuclei and, therefore, excludes nuclei such as tritium and thallium. Can. J. Biochem. Cell Biol. Downloaded from www.nrcresearchpress.com by University of Alberta on 08/03/15For personal use only.

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Phosphorus-31 nuclear magnetic resonance studies of adenosine 5'-triphosphate bound to a nitrated derivative of G-actin

Cited by 35 publications

References 36 publications

Tightly-bound divalent cation of actin

Tightly-bound divalent cation of actin

Structure of actin observed by fluorescence resonance energy transfer spectroscopy

Applications of ³¹P nuclear magnetic resonance to studies of protein structure and function

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Phosphorus-31 nuclear magnetic resonance studies of adenosine 5'-triphosphate bound to a nitrated derivative of G-actin

Cited by 35 publications

References 36 publications

Tightly-bound divalent cation of actin

Tightly-bound divalent cation of actin

Structure of actin observed by fluorescence resonance energy transfer spectroscopy

Applications of 31P nuclear magnetic resonance to studies of protein structure and function

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Applications of ³¹P nuclear magnetic resonance to studies of protein structure and function