東華大學圖書館 |

Language: English

Help

回圖書館首頁

手機版館藏查詢

Back to Search results for [ null ]

Switch To: Labeled | MARC Mode | ISBD

Ubiquitination mediated by RING fing...

Chen, Angus.

Linked to FindBook

Google Book

Amazon

博客來

Ubiquitination mediated by RING finger E3 ligases.

Record Type:	Electronic resources : Monograph/item
Title/Author:	Ubiquitination mediated by RING finger E3 ligases./
Author:	Chen, Angus.
Description:	133 p.
Notes:	Source: Dissertation Abstracts International, Volume: 63-02, Section: B, page: 7810.
Contained By:	Dissertation Abstracts International63-02B.
Subject:	Biochemistry. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3043108
ISBN:	9780493566573

Ubiquitination mediated by RING finger E3 ligases.
Chen, Angus.

Ubiquitination mediated by RING finger E3 ligases. - 133 p.

Source: Dissertation Abstracts International, Volume: 63-02, Section: B, page: 7810.

Thesis (Ph.D.)--Mount Sinai School of Medicine of New York University, 2002.

Ubiquitination, as a post-translational modification, regulates a variety of cellular processes. E3 ubiquitin ligases, the key component of the ubiquitination machinery, recruit an E2 to orchestrate the transfer of ubiquitin on to a bound substrate. A subset of the RING finger family, defined by conserved cysteine and histidine residues that coordinate zinc, are E3 ligases. Presented here is a biochemical study of two RING finger E3's, ROC1 and BRCA1/BARD1.

ISBN: 9780493566573Subjects--Topical Terms:

518028
Biochemistry.

Ubiquitination mediated by RING finger E3 ligases.
LDR:03477nmm a2200313 4500 001 2076039
005 20161101084223.5
008 170521s2002 ||||||||||||||||| ||eng d
020 $a 9780493566573
035 $a (MiAaPQ)AAI3043108
035 $a AAI3043108
040 $a MiAaPQ $c MiAaPQ
100 1 $a Chen, Angus. $3 3191469
245 1 0 $a Ubiquitination mediated by RING finger E3 ligases.
300 $a 133 p.
500 $a Source: Dissertation Abstracts International, Volume: 63-02, Section: B, page: 7810.
500 $a Adviser: Zhen-Qiang Pan.
502 $a Thesis (Ph.D.)--Mount Sinai School of Medicine of New York University, 2002.
520 $a Ubiquitination, as a post-translational modification, regulates a variety of cellular processes. E3 ubiquitin ligases, the key component of the ubiquitination machinery, recruit an E2 to orchestrate the transfer of ubiquitin on to a bound substrate. A subset of the RING finger family, defined by conserved cysteine and histidine residues that coordinate zinc, are E3 ligases. Presented here is a biochemical study of two RING finger E3's, ROC1 and BRCA1/BARD1.
520 $a ROC1 is a common component of an E3 family that includes the SCF, which primarily regulates the G1/S transition, and the VCB, which regulates hypoxia-inducible factors. Evidence is presented suggesting that a conserved RING-H2 structure within ROC1 is critical for its ubiquitination activity. Mercury-containing sulfhydryl modification agents irreversibly inhibit the ROC1/CUL1 ubiquitin ligase without disrupting the complex. Consistent with this, these reagents also eliminate the ability of the SCFHOS-ROC1 to support IkappaBalpha ubiquitination. Site-directed mutagenesis analysis identifies RING-H2 finger residues as essential for ROC1dependent ubiquitination. Furthermore, while some RING-H2 mutations reduce the ability of ROC1 to interact with CUL1 in transfected cells and of ROC1/CUL1 to form a stable complex with Cdc34 in vitro, other substitutions have no detectable effect on ROC1 binding activities. Thus, the ROC1 RING-H2 finger may possess multiple biochemical properties, including stabilizing the interaction with CUL1 and recruiting Cdc34.
520 $a The RING finger of BRCA1 confers ubiquitin ligase activity that is enhanced when complexed with another RING-containing protein, BARD1, and is required for this tumor suppressor protein in protecting genomic integrity. It is demonstrated that co-expression of BRCA1 and BARD 1 in bacteria assembles a potent ubiquitin ligase. Purified BRCA1/BARD1 stimulated the Ubc5c-mediated mono-ubiquitination of histone H2A(X) in vitro, suggesting a possible role for BRCA1/BARD1 in chromatin remodeling. Moreover, BRCA1/BARD1 auto-ubiquitinated efficiently in vitro, assembling non-lysine 48-linked polyubiquitin chains on the complex. When co-expressed in cells by transient transfection, the recombinant BRCA1/BARD1 complex was associated with polyubiquitin chains, suggesting that BRCA1/BARD1 was ubiquitinated in vivo as well. These results raise the possibility that BRCA1/BARD1 assembles non-lysine 48-linked polyubiquitin chains that may serve as a signaling platform required for coordinating DNA repair-related events.
590 $a School code: 1353.
650 4 $a Biochemistry. $3 518028
650 4 $a Cellular biology. $3 3172791
650 4 $a Molecular biology. $3 517296
690 $a 0487
690 $a 0379
690 $a 0307
710 2 $a Mount Sinai School of Medicine of New York University. $3 1025278
773 0 $t Dissertation Abstracts International $g 63-02B.
790 $a 1353
791 $a Ph.D.
792 $a 2002
793 $a English
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3043108