Literature DB >> 11473577

AAA+ superfamily ATPases: common structure--diverse function.

T Ogura1, A J Wilkinson.   

Abstract

The AAA+ superfamily of ATPases, which contain a homologous ATPase module, are found in all kingdoms of living organisms where they participate in diverse cellular processes including membrane fusion, proteolysis and DNA replication. Recent structural studies have revealed that they usually form ring-shaped oligomers, which are crucial for their ATPase activities and mechanisms of action. These ring-shaped oligomeric complexes are versatile in their mode of action, which collectively seem to involve some form of disruption of molecular or macromolecular structure; unfolding of proteins, disassembly of protein complexes, unwinding of DNA, or alteration of the state of DNA-protein complexes. Thus, the AAA+ proteins represent a novel type of molecular chaperone. Comparative analyses have also revealed significant similarities and differences in structure and molecular mechanism between AAA+ ATPases and other ring-shaped ATPases.

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Year:  2001        PMID: 11473577     DOI: 10.1046/j.1365-2443.2001.00447.x

Source DB:  PubMed          Journal:  Genes Cells        ISSN: 1356-9597            Impact factor:   1.891


  333 in total

1.  AAA proteins: in search of a common molecular basis. International Meeting on Cellular Functions of AAA Proteins.

Authors:  M R Maurizi; C C Li
Journal:  EMBO Rep       Date:  2001-11       Impact factor: 8.807

2.  Cooperative kinetics of both Hsp104 ATPase domains and interdomain communication revealed by AAA sensor-1 mutants.

Authors:  Douglas A Hattendorf; Susan L Lindquist
Journal:  EMBO J       Date:  2002-01-15       Impact factor: 11.598

3.  Analysis of the AAA sensor-2 motif in the C-terminal ATPase domain of Hsp104 with a site-specific fluorescent probe of nucleotide binding.

Authors:  Douglas A Hattendorf; Susan L Lindquist
Journal:  Proc Natl Acad Sci U S A       Date:  2002-02-26       Impact factor: 11.205

4.  MecA, an adaptor protein necessary for ClpC chaperone activity.

Authors:  Tilman Schlothauer; Axel Mogk; David A Dougan; Bernd Bukau; Kürşad Turgay
Journal:  Proc Natl Acad Sci U S A       Date:  2003-02-21       Impact factor: 11.205

5.  Conserved stem II of the box C/D motif is essential for nucleolar localization and is required, along with the 15.5K protein, for the hierarchical assembly of the box C/D snoRNP.

Authors:  Nicholas J Watkins; Achim Dickmanns; Reinhard Lührmann
Journal:  Mol Cell Biol       Date:  2002-12       Impact factor: 4.272

6.  Direct binding of ubiquitin conjugates by the mammalian p97 adaptor complexes, p47 and Ufd1-Npl4.

Authors:  Hemmo H Meyer; Yanzhuang Wang; Graham Warren
Journal:  EMBO J       Date:  2002-11-01       Impact factor: 11.598

7.  The rice (Oryza sativa L.) LESION MIMIC RESEMBLING, which encodes an AAA-type ATPase, is implicated in defense response.

Authors:  Rym Fekih; Muluneh Tamiru; Hiroyuki Kanzaki; Akira Abe; Kentaro Yoshida; Eiko Kanzaki; Hiromasa Saitoh; Hiroki Takagi; Satoshi Natsume; Jerwin R Undan; Jesusa Undan; Ryohei Terauchi
Journal:  Mol Genet Genomics       Date:  2014-11-04       Impact factor: 3.291

8.  Characterization of Alu and recombination-associated motifs mediating a large homozygous SPG7 gene rearrangement causing hereditary spastic paraplegia.

Authors:  Eva López; Carlos Casasnovas; Javier Giménez; Antoni Matilla-Dueñas; Ivelisse Sánchez; Víctor Volpini
Journal:  Neurogenetics       Date:  2014-11-16       Impact factor: 2.660

9.  GmFtsH9 expression correlates with in vivo photosystem II function: chlorophyll a fluorescence transient analysis and eQTL mapping in soybean.

Authors:  Zhitong Yin; Fanfan Meng; Haina Song; Xiaolin Wang; Maoni Chao; Guozheng Zhang; Xiaoming Xu; Dexiang Deng; Deyue Yu
Journal:  Planta       Date:  2011-06-03       Impact factor: 4.116

10.  Walker-A threonine couples nucleotide occupancy with the chaperone activity of the AAA+ ATPase ClpB.

Authors:  Maria Nagy; Hui-Chuan Wu; Zhonghua Liu; Sabina Kedzierska-Mieszkowska; Michal Zolkiewski
Journal:  Protein Sci       Date:  2009-02       Impact factor: 6.725

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