Literature DB >> 18208389

AAA+ proteins: diversity in function, similarity in structure.

Jamie Snider1, Walid A Houry.   

Abstract

The AAA+ (ATPases associated with various cellular activities) superfamily of proteins represents a distinct lineage of the larger class of P-loop NTPases. Members of this superfamily use the power of nucleotide binding and hydrolysis to direct molecular remodelling events. All AAA+ proteins share a common core architecture, which, through various sequence and structural modifications, has been adapted for use in a remarkably diverse range of functions. The following mini-review provides a concise description of the major structural elements common to all AAA+ proteins in the context of their mechanistic roles. In addition, the evolutionary and functional diversity of this superfamily is described on the basis of recent classification studies.

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Year:  2008        PMID: 18208389     DOI: 10.1042/BST0360072

Source DB:  PubMed          Journal:  Biochem Soc Trans        ISSN: 0300-5127            Impact factor:   5.407


  64 in total

1.  Binding of the ClpA unfoldase opens the axial gate of ClpP peptidase.

Authors:  Grégory Effantin; Michael R Maurizi; Alasdair C Steven
Journal:  J Biol Chem       Date:  2010-03-16       Impact factor: 5.157

2.  Gene mdpC plays a regulatory role in the methyl-tert-butyl ether degradation pathway of Methylibium petroleiphilum strain PM1.

Authors:  Geetika Joshi; Radomir Schmidt; Kate M Scow; Michael S Denison; Krassimira R Hristova
Journal:  FEMS Microbiol Lett       Date:  2015-02-26       Impact factor: 2.742

3.  The microtubule plus-end localization of Aspergillus dynein is important for dynein-early-endosome interaction but not for dynein ATPase activation.

Authors:  Jun Zhang; Lei Zhuang; Young Lee; Juan F Abenza; Miguel A Peñalva; Xin Xiang
Journal:  J Cell Sci       Date:  2010-09-28       Impact factor: 5.285

4.  Crystallization and preliminary X-ray analysis of the ATPase domain of the σ(54)-dependent transcription activator NtrC1 from Aquifex aeolicus bound to the ATP analog ADP-BeFx.

Authors:  Tatyana A Sysoeva; Neela Yennawar; Marc Allaire; B Tracy Nixon
Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun       Date:  2013-11-29

5.  Microtubule severing by katanin p60 AAA+ ATPase requires the C-terminal acidic tails of both α- and β-tubulins and basic amino acid residues in the AAA+ ring pore.

Authors:  Ai Johjima; Kentaro Noi; Shingo Nishikori; Hirotsugu Ogi; Masatoshi Esaki; Teru Ogura
Journal:  J Biol Chem       Date:  2015-03-24       Impact factor: 5.157

6.  Analysis of the cooperative ATPase cycle of the AAA+ chaperone ClpB from Thermus thermophilus by using ordered heterohexamers with an alternating subunit arrangement.

Authors:  Takashi Yamasaki; Yukiko Oohata; Toshiki Nakamura; Yo-hei Watanabe
Journal:  J Biol Chem       Date:  2015-02-24       Impact factor: 5.157

7.  An arginine tetrad as mediator of input-dependent and input-independent ATPases in the clock protein KaiC.

Authors:  Rekha Pattanayek; Yao Xu; Aashish Lamichhane; Carl H Johnson; Martin Egli
Journal:  Acta Crystallogr D Biol Crystallogr       Date:  2014-04-30

8.  Assembly-disassembly is coupled to the ATPase cycle of tobacco Rubisco activase.

Authors:  Andrew J Serban; Isabella L Breen; Hoang Q Bui; Marcia Levitus; Rebekka M Wachter
Journal:  J Biol Chem       Date:  2018-10-23       Impact factor: 5.157

9.  Regulation of ribulose-1,5-bisphosphate carboxylase/oxygenase (rubisco) activase: product inhibition, cooperativity, and magnesium activation.

Authors:  Suratna Hazra; J Nathan Henderson; Kevin Liles; Matthew T Hilton; Rebekka M Wachter
Journal:  J Biol Chem       Date:  2015-08-17       Impact factor: 5.157

10.  Comparative sequence analysis of a multidrug-resistant plasmid from Aeromonas hydrophila.

Authors:  Carmelo S Del Castillo; Jun-Ichi Hikima; Ho-Bin Jang; Seong-Won Nho; Tae-Sung Jung; Janenuj Wongtavatchai; Hidehiro Kondo; Ikuo Hirono; Haruko Takeyama; Takashi Aoki
Journal:  Antimicrob Agents Chemother       Date:  2012-10-15       Impact factor: 5.191

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