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Structures, dynamics, and interactions with UBC9 of the RING and B1‐box domains of promyelocytic leukemia protein (938.1)
Author(s) -
Huang Taihuang,
Huang ShuYu,
Naik Mandar
Publication year - 2014
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.28.1_supplement.938.1
Subject(s) - promyelocytic leukemia protein , sumo protein , rnf4 , ring finger , ring finger domain , microbiology and biotechnology , death associated protein 6 , chemistry , ubiquitin ligase , chromatin , zinc finger , dna binding domain , acute promyelocytic leukemia , biology , transcription factor , dna , ubiquitin , nuclear protein , biochemistry , retinoic acid , gene
PML protein is mainly present inside the nucleus in the form of PML nuclear bodies (PML‐NB) and serves as anchoring point for various sumoylated transcription factors and regulators. It mediates activities, such as transcriptional regulation, antiviral defense, DNA replication, DNA repair, telomere lengthening, chromatin organization, cell cycle control, senescence, apoptosis, and tumor suppression. PML‐NB is associated with acute promyelocytic leukemia (APL). All known isoforms of PML have conserved N‐terminal RBCC region comprised of a RING finger domain followed by two B‐boxes and coiled‐coil region. The RING domain has been shown to possess SUMO E3 ligase activity and the B1‐box can be poly‐sumoylated. Both the RING domain and the B1‐box are zinc finger proteins. Surprisingly, only the structure of the RING domain was determined in 1995 and no information on the structure of other part of the molecule is known. Here we will present the solution NMR structures and dynamics of the RING domain and the B1 box, as well as their interactions with Ubc9, SUMO and SUMO substrates. Grant Funding Source : Supported by a Grants NSC 101‐2311‐B‐001‐025 from The National Science Council