Control of meiotic pairing and recombination by chromosomally tethered 26S proteasome

Science

Volumn 355, Issue 6323, 2017, Pages 408-411

  Ahuja, Jasvinder S ^a   Sandhu, Rima ^a   Mainpal, Rana ^b   Lawson, Crystal ^c   Henley, Hanna ^a   Hunt, Patricia A ^c   Yanowitz, Judith L ^b   Valentin Borner G ^a,d,e  

^a CLEVELAND STATE UNIVERSITY   (United States)

^b UNIVERSITY OF PITTSBURGH   (United States)

^c WASHINGTON STATE UNIVERSITY   (United States)

^d CASE WESTERN RESERVE UNIVERSITY   (United States)

^e LERNER RESEARCH INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

MAMMALIA;

ATP DEPENDENT 26S PROTEASE; BENZYLOXYCARBONYLLEUCYL-LEUCYL-LEUCINE ALDEHYDE; CYSTEINE PROTEINASE INHIBITOR; LEUPEPTIN; NUCLEAR PROTEIN; PROTEASOME; SACCHAROMYCES CEREVISIAE PROTEIN; UBIQUITIN PROTEIN LIGASE; ZIP1 PROTEIN, S CEREVISIAE; ZIP3 PROTEIN, S CEREVISIAE;

CELL NUCLEUS; CHROMOSOME; CHROMOSOME PAIRING; CROSSING OVER; CYTOLOGY; CYTOPLASM; DOUBLE STRANDED DNA BREAK; ENZYMOLOGY; GENETICS; MEIOSIS; METABOLISM; MOLECULAR EVOLUTION; PHYSIOLOGY; PROTEIN DEGRADATION; SACCHAROMYCES CEREVISIAE; SYNAPTONEMAL COMPLEX;

CELL NUCLEUS; CHROMOSOME PAIRING; CHROMOSOMES, FUNGAL; CROSSING OVER, GENETIC; CYSTEINE PROTEINASE INHIBITORS; CYTOPLASM; DNA BREAKS, DOUBLE-STRANDED; EVOLUTION, MOLECULAR; LEUPEPTINS; MEIOSIS; NUCLEAR PROTEINS; PROTEASOME ENDOPEPTIDASE COMPLEX; PROTEOLYSIS; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; SYNAPTONEMAL COMPLEX; UBIQUITIN-PROTEIN LIGASES;

EID: 85008702761     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.aaf4778     Document Type: Article

References (26)

1. D. Zickler, N. Kleckner, Cold Spring Harb. Perspect. Biol. 7, a016626 (2015).
2. T. Tsubouchi, G. S. Roeder, Science 308, 870–873 (2005).
3. D. Obeso, R. J. Pezza, D. Dawson, Chromosoma 123, 43–55 (2014).
4. D. Obeso, D. S. Dawson, PLOS ONE 5, e10336 (2010).
5. G. V. Börner, N. Kleckner, N. Hunter, Cell 117, 29–45 (2004).
6. C. M. Lake, R. S. Hawley, Semin. Cell Dev. Biol. 54, 117–125 (2016).
7. J. Perry, N. Kleckner, G. V. Börner, Proc. Natl. Acad. Sci. U.S.A. 102, 17594–17599 (2005).
8. M. H. Glickman, A. Ciechanover, Physiol. Rev. 82, 373–428 (2002).
9. I. Velichutina, P. L. Connerly, C. S. Arendt, X. Li, M. Hochstrasser, EMBO J. 23, 500–510 (2004).
10. G. A. Brar et al., Science 335, 552–557 (2012).
11. M. A. Wilson, S. Meaux, A. van Hoof, Genetics 177, 773–784 (2007).
12. Materials and methods are available as supplementary materials.
13. E. Martini, R. L. Diaz, N. Hunter, S. Keeney, Cell 126, 285–295 (2006).
14. T. Tsubouchi, A. J. Macqueen, G. S. Roeder, Genes Dev. 22, 3217–3226 (2008).
15. A. V. Smith, G. S. Roeder, J. Cell Biol. 136, 957–967 (1997).
16. M. E. Serrentino, E. Chaplais, V. Sommermeyer, V. Borde, PLOS Genet. 9, e1003416 (2013).
17. S. Ben-Aroya et al., PLOS Genet. 6, e1000852 (2010).
18. R. J. Tomko Jr., M. Hochstrasser, Mol. Cell 44, 907–917 (2011).
19. T. S. McCann, W. P. Tansey, Biomolecules 4, 1026–1044 (2014).
20. W. Goodyer et al., Dev. Cell 14, 263–274 (2008).
21. K. Nabeshima, A. M. Villeneuve, M. P. Colaiácovo, J. Cell Biol. 168, 683–689 (2005).
22. H. B. D. Prasada Rao et al., Science 355, 403–407 (2017).
23. A. Zhang et al., J. Biol. Chem. 281, 35997–36003 (2006).
24. N. J. Krogan et al., Mol. Cell 16, 1027–1034 (2004).
25. L. Zhang et al., Nature 511, 551–556 (2014).
26. G. A. Brar, A. Hochwagen, L. S. Ee, A. Amon, Mol. Biol. Cell 20, 1030–1047 (2009).