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TRIP13 is a protein-remodeling AAA+ ATPase that catalyzes MAD2 conformation switching

Ye, Qiaozhen ; Rosenberg, Scott C ; Moeller, Arne ; Speir, Jeffrey A ; Su, Tiffany Y ; Corbett, Kevin D

eLife, 2015-04, Vol.4 [Periódico revisado por pares]

England: eLife Sciences Publications Ltd

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Título:
TRIP13 is a protein-remodeling AAA+ ATPase that catalyzes MAD2 conformation switching
Autor: Ye, Qiaozhen ; Rosenberg, Scott C ; Moeller, Arne ; Speir, Jeffrey A ; Su, Tiffany Y ; Corbett, Kevin D
Assuntos: AAA+ ATPase ; Adaptor Proteins, Signal Transducing - chemistry ; Adaptor Proteins, Signal Transducing - genetics ; Adaptor Proteins, Signal Transducing - metabolism ; Adenosine triphosphatase ; Adenosine Triphosphatases - chemistry ; Adenosine Triphosphatases - genetics ; Adenosine Triphosphatases - metabolism ; Amino Acid Sequence ; Animals ; ATPases Associated with Diverse Cellular Activities ; BASIC BIOLOGICAL SCIENCES ; Biochemistry ; Biophysics and Structural Biology ; Caenorhabditis elegans - classification ; Caenorhabditis elegans - enzymology ; Caenorhabditis elegans - genetics ; Caenorhabditis elegans Proteins - chemistry ; Caenorhabditis elegans Proteins - genetics ; Caenorhabditis elegans Proteins - metabolism ; Carrier Proteins - chemistry ; Carrier Proteins - genetics ; Carrier Proteins - metabolism ; Cell Cycle Proteins - chemistry ; Cell Cycle Proteins - genetics ; Cell Cycle Proteins - metabolism ; Chromosomes ; Crystallography, X-Ray ; Deoxyribonucleic acid ; DNA ; DNA repair ; Endopeptidase Clp - chemistry ; Endopeptidase Clp - genetics ; Endopeptidase Clp - metabolism ; Escherichia coli - genetics ; Escherichia coli - metabolism ; Escherichia coli Proteins - chemistry ; Escherichia coli Proteins - genetics ; Escherichia coli Proteins - metabolism ; Gene Expression ; HORMA domain protein ; Humans ; M Phase Cell Cycle Checkpoints ; Mad2 Proteins - chemistry ; Mad2 Proteins - genetics ; Mad2 Proteins - metabolism ; Mammals ; Medical research ; Meiosis ; Models, Molecular ; Molecular Chaperones - chemistry ; Molecular Chaperones - genetics ; Molecular Chaperones - metabolism ; Molecular Sequence Data ; N-Ethylmaleimide-Sensitive Proteins - chemistry ; N-Ethylmaleimide-Sensitive Proteins - genetics ; N-Ethylmaleimide-Sensitive Proteins - metabolism ; Nuclear Proteins - chemistry ; Nuclear Proteins - genetics ; Nuclear Proteins - metabolism ; Phylogeny ; Protein Binding ; Protein Structure, Tertiary ; Proteins ; Recombinant Proteins - chemistry ; Recombinant Proteins - genetics ; Recombinant Proteins - metabolism ; Recombination ; Sequence Alignment ; Sequence Homology, Amino Acid ; Software ; Spindle Apparatus - enzymology ; Spindle Apparatus - genetics ; spindle assembly checkpoint
É parte de: eLife, 2015-04, Vol.4
Notas: ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
March of Dimes Foundation
R01GM10414; P41GM103393; GM103310; FY14-251
National Institutes of Health (NIH)
USDOE Office of Science (SC), Biological and Environmental Research (BER)
Sidney Kimmel Foundation for Cancer Research
Descrição: The AAA+ family ATPase TRIP13 is a key regulator of meiotic recombination and the spindle assembly checkpoint, acting on signaling proteins of the conserved HORMA domain family. Here we present the structure of the Caenorhabditis elegans TRIP13 ortholog PCH-2, revealing a new family of AAA+ ATPase protein remodelers. PCH-2 possesses a substrate-recognition domain related to those of the protein remodelers NSF and p97, while its overall hexameric architecture and likely structural mechanism bear close similarities to the bacterial protein unfoldase ClpX. We find that TRIP13, aided by the adapter protein p31(comet), converts the HORMA-family spindle checkpoint protein MAD2 from a signaling-active 'closed' conformer to an inactive 'open' conformer. We propose that TRIP13 and p31(comet) collaborate to inactivate the spindle assembly checkpoint through MAD2 conformational conversion and disassembly of mitotic checkpoint complexes. A parallel HORMA protein disassembly activity likely underlies TRIP13's critical regulatory functions in meiotic chromosome structure and recombination.
Editor: England: eLife Sciences Publications Ltd
Idioma: Inglês

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TRIP13 is a protein-remodeling AAA+ ATPase that catalyzes MAD2 conformation switching

Ye, Qiaozhen ; Rosenberg, Scott C ; Moeller, Arne ; Speir, Jeffrey A ; Su, Tiffany Y ; Corbett, Kevin D

England: eLife Sciences Publications Ltd

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