The Molybdenum Storage Protein: A soluble ATP hydrolysis-dependent molybdate pump

Poppe J, Bruenle S, Hail R, Wiesemann K, Schneider K, Ermler U (2018)
FEBS JOURNAL 285(24): 4602-4616.

Zeitschriftenaufsatz | Veröffentlicht | Englisch
 
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Autor*in
Poppe, Juliane; Bruenle, Steffen; Hail, Ron; Wiesemann, Katharina; Schneider, KlausUniBi; Ermler, Ulrich
Abstract / Bemerkung
A continuous FeMo cofactor supply for nitrogenase maturation is ensured in Azotobacter vinelandii by developing a cage-like molybdenum storage protein (MoSto) capable to store ca. 120 molybdate molecules (MoO42-) as discrete polyoxometalate (POM) clusters. To gain mechanistic insight into this process, MoSto was characterized by Mo and ATP/ADP content, structural, and kinetic analysis. We defined three functionally relevant states specified by the presence of both ATP/ADP and POM clusters (MoSto(funct)), of only ATP/ADP (MoSto(basal)) and of neither ATP/ADP nor POM clusters (MoSto(zero)), respectively. POM clusters are only produced when ATP is hydrolyzed to ADP and phosphate. V-max was ca. 13 mu mol(phosphate).min(-1).mg(-1) and K-m for molybdate and ATP/Mg2+ in the low micromolar range. ATP hydrolysis presumably proceeds at subunit alpha, inferred from a highly occupied alpha-ATP/Mg2+ and a weaker occupied beta-ATP/no Mg2+-binding site found in the MoSto(funct) structure. Several findings indicate that POM cluster storage is separated into a rapid ATP hydrolysis-dependent molybdate transport across the protein cage wall and a slow molybdate assembly induced by combined auto-catalytic and protein-driven processes. The cage interior, the location of the POM cluster depot, is locked in all three states and thus not rapidly accessible for molybdate from the outside. Based on V-max, the entire Mo storage process should be completed in less than 10 s but requires, according to the molybdate content analysis, ca. 15 min. Long-time incubation of MoSto(basal) with nonphysiological high molybdate amounts implicates an equilibrium in and outside the cage and POM cluster self-formation without ATP hydrolysis.
Erscheinungsjahr
2018
Zeitschriftentitel
FEBS JOURNAL
Band
285
Ausgabe
24
Seite(n)
4602-4616
ISSN
1742-464X
eISSN
1742-4658
Page URI
https://pub.uni-bielefeld.de/record/2932970

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Poppe J, Bruenle S, Hail R, Wiesemann K, Schneider K, Ermler U. The Molybdenum Storage Protein: A soluble ATP hydrolysis-dependent molybdate pump. FEBS JOURNAL. 2018;285(24):4602-4616.
Poppe, J., Bruenle, S., Hail, R., Wiesemann, K., Schneider, K., & Ermler, U. (2018). The Molybdenum Storage Protein: A soluble ATP hydrolysis-dependent molybdate pump. FEBS JOURNAL, 285(24), 4602-4616. doi:10.1111/febs.14684
Poppe, J., Bruenle, S., Hail, R., Wiesemann, K., Schneider, K., and Ermler, U. (2018). The Molybdenum Storage Protein: A soluble ATP hydrolysis-dependent molybdate pump. FEBS JOURNAL 285, 4602-4616.
Poppe, J., et al., 2018. The Molybdenum Storage Protein: A soluble ATP hydrolysis-dependent molybdate pump. FEBS JOURNAL, 285(24), p 4602-4616.
J. Poppe, et al., “The Molybdenum Storage Protein: A soluble ATP hydrolysis-dependent molybdate pump”, FEBS JOURNAL, vol. 285, 2018, pp. 4602-4616.
Poppe, J., Bruenle, S., Hail, R., Wiesemann, K., Schneider, K., Ermler, U.: The Molybdenum Storage Protein: A soluble ATP hydrolysis-dependent molybdate pump. FEBS JOURNAL. 285, 4602-4616 (2018).
Poppe, Juliane, Bruenle, Steffen, Hail, Ron, Wiesemann, Katharina, Schneider, Klaus, and Ermler, Ulrich. “The Molybdenum Storage Protein: A soluble ATP hydrolysis-dependent molybdate pump”. FEBS JOURNAL 285.24 (2018): 4602-4616.

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Genetic and Biochemical Analysis of the Azotobacter vinelandii Molybdenum Storage Protein.
Navarro-Rodríguez M, Buesa JM, Rubio LM., Front Microbiol 10(), 2019
PMID: 30984129

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