Ubiquitin E3 ligase

Chemistry: molecular biology and microbiology – Measuring or testing process involving enzymes or... – Involving hydrolase

Reexamination Certificate

Rate now

  [ 0.00 ] – not rated yet Voters 0   Comments 0

Details

Reexamination Certificate

active

07923219

ABSTRACT:
The present invention provides a native or reconstituted complex comprising Bmi1 and/or Ring1 and/or Ring2, wherein the complex has ubiquitin E3 ligase activity. Optionally, the complex further comprises HPH2 and/or HPC3. Also disclosed are methods of producing the reconstituted complex, methods of identifying compounds that modulate the ubiquitin E3 ligase activity of the native or reconstituted complex, and methods of identifying candidate compounds for treating cancer. Kits for determining modulation of protein ubiquitination and/or for ubiquitinating a target substrate are further provided.

REFERENCES:
patent: 6737244 (2004-05-01), Issakani et al.
patent: 6740495 (2004-05-01), Issakani et al.
patent: 6919184 (2005-07-01), Issakani et al.
patent: 2004/0137597 (2004-07-01), Davydov et al.
patent: 2005/0009871 (2005-01-01), Ramesh et al.
patent: 2005/0032139 (2005-02-01), Issakani et al.
patent: WO 2004/052392 (2004-06-01), None
patent: WO 2004/052392 (2004-06-01), None
Wang et al. Role of Histone H2A Ubiquitination in Polycomb Silencing. Nature vol. 413, Oct. 2004, 873-878.
Capili A. et al. Structure of the C-Terminal RING Finger . . . J Molecular Biology 340(5)1117-1129, Jul. 23, 2004.
Kenten J. et al. Assays for High Throughput Screening of E2 and E3 Ubiquitin Ligases. Methods in Enzymology 399:682-700, 2005.
Wang H. et al. Role of Histone H2A Ubiqutination of Polycomb Silencing. Nature 431:873-878, Oct. 14, 2004.
Francis et al.; “Reconstitution of a Functional Core Polycomb Repressive Complex,”Molecular Cell, vol. 8 (Sep. 2001), p. 545-556.
J. Horn et al., “RING protein Trim32 associated with skin carcinogenesis has anti-apoptotic and E3-ubiquitin ligase properties,”Carcinogenesis, vol. 25, No. 2 (2004), p. 157-167.
Joazeiro et al., “RING Finger Proteins: Mediators of Ubiquitin Ligase Activity,”Cell, vol. 102 (Sep. 1, 2000), p. 549-552.
Kenten et al., “Assays for High-Throughput Screening of E2 and E3 Ubiquitin Ligases,”Methods in Enzymology, vol. 399 (2005), p. 682-701.
Levine et al, “The Core of the Polycomb Repressive Complex Is Compositionally and Functionally Conserved in Files and Humans,”Molecular and Cellular Biology, vol. 22, No. 17 (Sep. 2002), p. 6070-6078.
Napoles et al., “Polycomb Group Proteins Ring1A/B Link Ubiquitylation of Histone H2A to Heritable Gene Silencing and X Inactivation,”Developmental Cell, vol. 7 (Nov. 2004), p. 663-675.
Otte et al., “Gene repression by Polycomb group protein complexes: a distinct complex for every occasion?”Current Opinion in Genetics&Development, vol. 13 (2003), p. 448-454.
Passmore et al., “Getting into position: the catalytic mechanisms of protein ubiquitylation,”Biochem. J., vol. 379, (2004), p. 513-525.
Ringrose et al., “Epigenetic Regulation of Cellular Memory by the Polycomb and Trithorax Group Proteins,”Annu. Rev. Genet., vol. 38 (2004), p. 413-43.
Satijn et al, “RING1 is Associatd with the Polycomb Group Protein Complex and Acts as a Transcriptional Repressor,”Molecular and Cellular Biology, vol. 17, No. 7 (Jul. 1997), p. 4105-4113.
Schloβherr et al., “Gene inactivation inDrosophilamediated by the Polycomb gene product or by position-effect variegation does not involve major changes in the accessibility of the chromatin fibre,”Mol Ge Genet, vol. 243 (1994), p. 453-462.
Schoorlemmer et al., “Ring1A is a transcriptional repressor that interacts with the Polycomb-M33 protein and is expressed at rhombomere boundaries in the mouse hindbrain,”The EMBO Journal, vol. 15, No. 19 (1997), p. 5930-5942.
Shao et al., “Stabilization of Chromatin Structure by PRC1, a Polycomb Complex,”Cell, vol. 98 (Jul. 9, 1999), p. 37-46.
Wang et al., “Hierarchical Recruitment of Polycomb Group Silencing Complexes,”Molecular Cell, vol. 14 (Jun. 4, 2004), 637-646.
Wang et al., “Role of histone H2A ubiquitination in Polycomb silencing,”Nature, vol. 431 (Oct. 14, 2004), p. 873-878.
Zhang, “No exception to reversibility,”Nature, vol. 431 (Oct. 7, 2004), p. 637-639.
Zhang, “Role of histone modifications in polycomb silencing and cellular memory,” Abstract presented at the Cold Spring Harbor 69thSymposium, (Jun. 2-7, 2004), 1 page.
Zhang, “Role of histone methylation and ubiquitination in PcG silencing,” Oral presentation, Cold Spring Harbor 69thSymposium: Epigenetics (Jun. 6, 2004), 30 pages.
NCBI Accession No. NM—007552Mus musculus Bmil polycomb ring finger oncogene, created Apr. 1, 2000.
NCBI Accession No. NM—005180Homo sapiens BMI1 polycomb finger oncogene, created May 24, 1999.
NCBI Accession No. NP—005171Polycomb group ring finger 4(Homo sapiens), created May 24, 1999.
NCBI Accession No. NP—031578Bmil polycomb ring finger oncogene, created Apr. 11, 2000.
International Search Report and the Written Opinion of the International Searching Authority for PCT Application No. PCT/US06/21159, mailed Feb. 6, 2007.
Extended European Search Report for European Application No. 06784518.0, Mailed Jul. 30, 2008.
Cao, R et al., “Role of Bmi-1 and Ring1A in H2A Ubiquitylation and Hox Gene Silencing”, Molecular Cell, Cell Press, Cambridge, MA, US, 20(6):845-854, Dec. 22, 2005. XP-002460133.
Hamer, Karien M. et al., “A Panel of Monoclonal Antibodies Against Human Polycomb Group Proteins”, Hybridoma and Hybridomics, Mary Ann Liebert, New York, N.Y., US, 21(4): 245-252, Aug. 1, 2002. XP008015767.
Wei, Jianhua et al.,“Role of Bmi1 in H2A Ubiquitylation and Hox Gene Silencing”, Journal of Biological Chemistry, 281(32): 22537-22544, Aug. 2006. XP002488667.
Zhang et al. “Mechanism of Polycomb Group Gene Silencing”Cold Spring Harbor Symposia on Quantitative BiologyLXIX:1-9 (2004).
Zhang et al. “Mechanism of Polycomb Group Gene Silencing”Cold Spring Harbor Symposia on Quantitative BiologyLXIX:1-9 (Oct. 25, 2004).

LandOfFree

Say what you really think

Search LandOfFree.com for the USA inventors and patents. Rate them and share your experience with other people.

Rating

Ubiquitin E3 ligase does not yet have a rating. At this time, there are no reviews or comments for this patent.

If you have personal experience with Ubiquitin E3 ligase, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Ubiquitin E3 ligase will most certainly appreciate the feedback.

Rate now

     

Profile ID: LFUS-PAI-O-2730458

  Search
All data on this website is collected from public sources. Our data reflects the most accurate information available at the time of publication.