Mechanisms of ATPases--a multi-disciplinary approach.
ATPases are important molecular machines that convert the chemical energies stored in ATP to mechanical actions within the cell. ATPases are among the most abundant proteins with diverse functions involved in almost every cellular pathway. The well characterised ATPases include the various motor proteins responsible for cargo transfers, cell motilities, and muscle contractions; the protein degradation machinery - the proteasome; the ATP synthase, F-ATPase; and the chaperone systems. Other ATPases include DNA helicases and DNA replication complex; proteins responsible for protein/complex disassembly; and certain gene regulators. It is beyond the scope of this review to cover the complete range of ATPases. Instead, we will focus on a few representative ATPases, chosen based on their diverse mechanisms and properties. Furthermore, this review is by no means trying to cover comprehensively the literature for each ATPase nor the historical aspects in each field. We will focus on describing the various techniques being employed to derive the mechanisms and properties of the chosen ATPases. Among them, high and low resolution structural studies combined with biochemical assays seem to be the dominant technical advances adapted to reveal mechanisms for most of the ATPases except the bacterial sigma54 activators, whose mechanism of action is mostly derived from large amount of biochemical studies. A number of them, especially the F-ATPase and motor proteins, have been studied successfully by various single molecule and imaging techniques. We will therefore discuss them in greater details in order to describe the wide range techniques being utilised.
Rappas
Mathieu
M
Centre for Structural Biology, Department of Biological Sciences, Imperial College London, Flowers Building, South Kensington London SW7 2AZ, UK.
Niwa
Hajime
H
Zhang
Xiaodong
X
D000251:Adenosine Triphosphatases / Q000737:chemistry* / Q000378:metabolism*; D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism; D018835:Chaperonin 10 / Q000737:chemistry / Q000378:metabolism; D018834:Chaperonin 60 / Q000737:chemistry / Q000378:metabolism; D004265:DNA Helicases / Q000737:chemistry / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000737:chemistry / Q000378:metabolism / Q000502:physiology; D012321:DNA-Directed RNA Polymerases / Q000737:chemistry / Q000378:metabolism / Q000502:physiology; D029968:Escherichia coli Proteins; D006801:Humans; D016547:Kinesins / Q000737:chemistry / Q000378:metabolism; D008565:Membrane Proteins / Q000737:chemistry / Q000378:metabolism; D025261:Mitochondrial Proton-Translocating ATPases / Q000737:chemistry / Q000378:metabolism; D008954:Models, Biological; D008958:Models, Molecular; D009687:Nuclear Proteins / Q000737:chemistry / Q000378:metabolism; D011487:Protein Conformation; D017510:Protein Folding; D006180:Proton-Translocating ATPases / Q000737:chemistry / Q000378:metabolism; D051877:RNA Polymerase Sigma 54; D012808:Sigma Factor / Q000737:chemistry / Q000378:metabolism / Q000502:physiology
D001426:Bacterial Proteins; D018835:Chaperonin 10; D018834:Chaperonin 60; D004268:DNA-Binding Proteins; D029968:Escherichia coli Proteins; D008565:Membrane Proteins; D009687:Nuclear Proteins; C061260:RuvB protein, Bacteria; D012808:Sigma Factor; D000255:Adenosine Triphosphate; D012321:DNA-Directed RNA Polymerases; D051877:RNA Polymerase Sigma 54; C071059:Holliday junction DNA helicase, E coli; D000251:Adenosine Triphosphatases; C474451:F1F0-ATP synthase; C103607:mitochondrial ATPase subunit c; C404942:p97 ATPase; D025261:Mitochondrial Proton-Translocating ATPases; C444660:gamma subunit, F(1) ATPase; D006180:Proton-Translocating ATPases; D004265:DNA Helicases; D016547:Kinesins