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  Atomic Structure of the KEOPS Complex: An Ancient Protein Kinase-Containing Molecular Machine

Mao, D. Y. L., Neculai, D., Downey, M., Orlicky, S., Haffani, Y. Z., Ceccarelli, D. F., et al. (2008). Atomic Structure of the KEOPS Complex: An Ancient Protein Kinase-Containing Molecular Machine. Molecular Cell, 32(2), 259-275. doi:10.1016/j.molcel.2008.10.002.

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 Creators:
Mao, Daniel Y. L.1, Author
Neculai, Dante1, Author
Downey, Michael1, 2, Author
Orlicky, Stephen1, Author
Haffani, Yosr Z.1, Author
Ceccarelli, Derek F.1, Author
Ho, Jenny S. L.3, Author
Szilard, Rachel K.1, Author
Zhang, Wei1, 2, Author
Ho, Cynthia S.1, Author
Wan, Leo1, Author
Farès, Christophe4, Author           
Rumpel, Sigrun4, Author
Kurinov , Igor5, Author
Arrowsmith , Cheryl H.4, Author
Durocher , Daniel1, 2, Author
Sicheri , Frank1, 2, Author
Affiliations:
1Samuel Lunenfeld Research Institute, Mount Sinai Hospital, 600 University Avenue, Toronto, ON, M5G 1X5, Canada, ou_persistent22              
2Department of Molecular Genetics, University of Toronto, Toronto, ON, M5S 1A8, Canada, ou_persistent22              
3Program in Developmental and Stem Cell Biology, The Hospital for Sick Children and University of Toronto, 555 University Avenue, Toronto, ON, M5G 1X8, Canada, ou_persistent22              
4Ontario Cancer Institute, Department of Medical Biophysics, University of Toronto, 101 College Street, Toronto, ON, M5G 1L7, Canada, ou_persistent22              
5Cornell University, Department of Chemistry and Chemical Biology, NE-CAT, Bldg. 436E, Advanced Photon Source, 9700 S. Cass Avenue, Argonne, IL 60439, USA, ou_persistent22              

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Free keywords: Proteins; DNA
 Abstract: Kae1 is a universally conserved ATPase and part of the essential gene set in bacteria. In archaea and eukaryotes, Kae1 is embedded within the protein kinase-containing KEOPS complex. Mutation of KEOPS subunits in yeast leads to striking telomere and transcription defects, but the exact biochemical function of KEOPS is not known. As a first step to elucidating its function, we solved the atomic structure of archaea-derived KEOPS complexes involving Kae1, Bud32, Pcc1, and Cgi121 subunits. Our studies suggest that Kae1 is regulated at two levels by the primordial protein kinase Bud32, which is itself regulated by Cgi121. Moreover, Pcc1 appears to function as a dimerization module, perhaps suggesting that KEOPS may be a processive molecular machine. Lastly, as Bud32 lacks the conventional substrate-recognition infrastructure of eukaryotic protein kinases including an activation segment, Bud32 may provide a glimpse of the evolutionary history of the protein kinase family.

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Language(s): eng - English
 Dates: 2008-08-192008-10-022008-10-212008-10-24
 Publication Status: Published in print
 Pages: 17
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/j.molcel.2008.10.002
 Degree: -

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Title: Molecular Cell
Source Genre: Journal
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Publ. Info: Cambridge, Mass. : Cell Press
Pages: - Volume / Issue: 32 (2) Sequence Number: - Start / End Page: 259 - 275 Identifier: ISSN: 1097-2765
CoNE: https://pure.mpg.de/cone/journals/resource/954925610929