Membrane sectors of F- and V-type H+-transporting ATPases

Current Opinion in Structural Biology

Volumn 6, Issue 4, 1996, Pages 491-498

  Fillingame, Robert H ^a  

^a UNIVERSITY OF WISCONSIN SCHOOL OF MEDICINE AND PUBLIC HEALTH   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE;

ENZYME MECHANISM; ENZYME STRUCTURE; ENZYME SUBUNIT; PRIORITY JOURNAL; PROTON TRANSPORT; REVIEW;

EID: 0030220656     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-440X(96)80114-X     Document Type: Article

References (58)

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21. V hexamer.
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23. + channel of vacuolar proton pumps. J Biol Chem. 269:1994;17379-17381.
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26. 0 domains of yeast vacuolar ATPase are shown to reversibly disassociate and reassociate upon removal and addition and glucose, respectively. The results support ideas on autonomous assembly of the two sectors and the results of biochemical and genetic experiments defining their subunit compositions.
27. +translocation. Here, it is shown that the essential arginine can be moved to position 252 with retention of function in the aArg210Gln/Gln252Arg mutant. The proposed juxtaposition of Arg210 in helix 4 and Gln252 in helix 5 supports previous suggestions that Gly218 and Gln219 of helix 4 may be juxtaposed to His245 of helix 5 [53,54].
28. 0 complexes of E. coli, and subcomplexes thereof, are analyzed by electron spectroscopic imaging. Modeling of the images suggests a structure in which subunit a and the two subunit bs locate to the outside of a subunit c oligomer.
29. o, embedded within the lipid bilayer and extending to only one side of the stalk. The authors suggest that the width of the very narrow stalk, provided by averaging of images, may be underestimated.
30. 1 sector. J Biol Chem. 267:1992;7630-7636.
31. o.
32. o ATP synthase. Biochem Soc Trans. 23:1995;760-766 Recent studies on NMR structure of subunit c are reviewed and aspects of structure are correlated with recent biochemical and genetic studies from my laboratory.
33. o subunit c. J Biol Chem. 270:1995;24609-24614 Cysteines introduced at positions 40, 41 and 42 of the polar loop of subunit c are shown to cross-link with Cys31 in the εE31C mutant and indicate a structural juxtaposition of the two regions. A functional interaction of the two regions had been predicted on the basis of εE31 suppressor mutations which corrected the uncoupled phenotype of the cQ42E mutant [55].
34. o). Biochem Soc Trans. 23:1995;767-770 The authors review recent studies from their laboratory that suggest movement of the γ and ε subunits during coupled ATP hydrolysis/synthesis. The structure of the ε subunit is also discussed.
35. 2+, the εS108C/βE381C crosslink is preferred. The results are consistent with the idea that γ and ε move from site to site to promote changes in catalytic-site occupancy.
36. o via one segment of the β structure, which includes His38 and Glu31. A second face of this domain, which lies at right angles to this plane, is predicted to interact with the γ subunit [38]. A second, helix-turn-helix domain at the C-terminal end of the protein is known to interact with the DELSEED region of subunit β, so subunit ε,must span the entire stalk.
37. o interface.
38. 1-ATPase. J Biol Chem. 271:1996;3018-3024 The interacting faces of the γ and ε subunits are further defined using a series of cysteine substitutions and cross-linking with a photoreactive, heterobifunctional maleimide.
39. 1 to the membrane. J Biol Chem. 263:1988;4619-4623.
40. 1 and the oligomycin-sensitivity conferral protein. Biochem J. 303:1994;639-645.
41. o function on introduction of mutant c lacking Asp61, the reconstitution experiments described show that subunit c retains full activity after purification in chloroform-methanol-water (4:4:1) solvent, i.e. the solvent used in the NMR studies of Girvin and Fillingame [42].
42. o ATP synthase. Biochemistry. 34:1995;1635-1645 A high-resolution structure for the interacting helices at the N- and C- terminal end of the helical hairpin of subunit c is determined after introduction of a spin label at Cys67 (Figure 3). The difference method identifies the local resonances broadened by the paramagnetic probe. The packing of helices and structure in the region around Asp61 are of particular interest.
43. +-translocating function retained. Proc Natl Acad Sci USA. 87:1990;4900-4904.
44. o ATP synthase: effect of position 61 substitutions in helix-2 on function of Asp24 in helix-1. J Biol Chem. 269:1994;5473-5479.
45. +-translocating carboxyl, is exceptionally high, as if the carboxyl group is shielded from solvent. The structural model suggests that the protonated carboxyl is buried in a pocket formed by hydrophobic side chains [42].
46. +.
47. + concentration: probing the binding site for the coupling ions. Biochemistry. 32:1993;10378-10386.
48. o-ATPase from Propionigenium modestum by dicyclohexylcarbodiimide. FEBS Lett. 340:1994;245-248.
49. + competed for transport. Cation chelation is proposed to occur via the substituted Glu61 and Ser62 side chains.
50. + ion.
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54. o ATP synthase in Escherichia coli. J Biol Chem. 269:1994;32313-32317.
55. o ATP synthase. J Biol Chem. 269:1994;10221-10224.
56. 2+ + ATP binding is determined by and/or helps to determine the interactions of different αβ pairs with γ and ε. This conclusion is in agreement with those discussed above [7].
57. 1). J Biol Chem. 263:1988;17437-17442.
58. 1-ATPase with subunit b dimer. FEBS Lett. 354:1994;37-40.