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Title: A Ubiquitin Ligase Transfers Preformed Polyubiquitin Chains From a Conjugating Enzyme to a Substrate

Abstract

No abstract prepared.

Authors:
; ; ; ; ; ;
Publication Date:
Research Org.:
Stanford Linear Accelerator Center (SLAC)
Sponsoring Org.:
USDOE
OSTI Identifier:
901829
Report Number(s):
SLAC-REPRINT-2007-025
TRN: US200717%%77
DOE Contract Number:
AC02-76SF00515
Resource Type:
Journal Article
Resource Relation:
Journal Name: Nature 446:333-337,2007; Journal Volume: 446
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; CHAINS; ENZYMES; LIGASES; SUBSTRATES; Other,OTHER

Citation Formats

Li, Wei, Tu, Daqi, /Natl. Inst. Health, Brunger, Axel T., /SLAC, SSRL, Ye, Yihong, and /Natl. Inst. Health. A Ubiquitin Ligase Transfers Preformed Polyubiquitin Chains From a Conjugating Enzyme to a Substrate. United States: N. p., 2007. Web. doi:10.1038/nature05542.
Li, Wei, Tu, Daqi, /Natl. Inst. Health, Brunger, Axel T., /SLAC, SSRL, Ye, Yihong, & /Natl. Inst. Health. A Ubiquitin Ligase Transfers Preformed Polyubiquitin Chains From a Conjugating Enzyme to a Substrate. United States. doi:10.1038/nature05542.
Li, Wei, Tu, Daqi, /Natl. Inst. Health, Brunger, Axel T., /SLAC, SSRL, Ye, Yihong, and /Natl. Inst. Health. Fri . "A Ubiquitin Ligase Transfers Preformed Polyubiquitin Chains From a Conjugating Enzyme to a Substrate". United States. doi:10.1038/nature05542.
@article{osti_901829,
title = {A Ubiquitin Ligase Transfers Preformed Polyubiquitin Chains From a Conjugating Enzyme to a Substrate},
author = {Li, Wei and Tu, Daqi and /Natl. Inst. Health and Brunger, Axel T. and /SLAC, SSRL and Ye, Yihong and /Natl. Inst. Health},
abstractNote = {No abstract prepared.},
doi = {10.1038/nature05542},
journal = {Nature 446:333-337,2007},
number = ,
volume = 446,
place = {United States},
year = {Fri Apr 06 00:00:00 EDT 2007},
month = {Fri Apr 06 00:00:00 EDT 2007}
}
  • Highlights: Black-Right-Pointing-Pointer We isolated a novel E2 ubiquitin-conjugating enzyme from leaves of wild rice plants. Black-Right-Pointing-Pointer The OgUBC1 was highly expressed in leaves treated with SA and UV-B radiation. Black-Right-Pointing-Pointer The recombinant OgUBC1 has an enzymatic activity of E2 in vitro. Black-Right-Pointing-Pointer The OgUBC1 could protect disruption of plant cells by UV-B radiation. Black-Right-Pointing-Pointer OgUBC1 confers disease resistance and UV-B tolerance in transgenic Arabidopsis plants. -- Abstract: A previously unidentified gene encoding ubiquitin-conjugating enzyme was isolated from leaves of wild rice plant treated with wounding and microbe-associated molecular patterns. The OgUBC1 gene was composed of 148 amino acids and containedmore » a typical active site and 21 ubiquitin thioester intermediate interaction residues and 4 E3 interaction residues. Both exogenous application of salicylic acid and UV-B irradiation triggered expression of OgUBC1 in leaves of wild rice. Recombinant OgUBC1 proteins bound to ubiquitins in vitro, proposing that the protein might act as E2 enzyme in planta. Heterologous expression of the OgUBC1 in Arabidopsis thaliana protected plants from cellular damage caused by an excess of UV-B radiation. A stable expression of chalcone synthase gene was detected in leaves of OgUBC1-expressing Arabidopsis, resulting in producing higher amounts of anthocyanin than those in wild-type Col-0 plants. Additionally, both pathogenesis-related gene1 and 5 were transcribed in the transgenic Arabidopsis in the absence of pathogen infection. The OgUBC1-expressing plants were resistant to the infection of Botrytis cinerea. Taken together, we suggested that the OgUBC1 is involved in ubiquitination process important for cellular response against biotic and abiotic stresses in plants.« less
  • Ubiquitination of proteins provides a powerful and versatile post-translational signal in the eukaryotic cell. The formation of a thioester bond between ubiquitin (Ub) and the active site of a ubiquitin-conjugating enzyme (E2) is critical for the transfer of Ub to substrates. Assembly of a functional ubiquitin ligase (E3) complex poised for Ub transfer involves recognition and binding of an E2~Ub conjugate. Therefore, full characterization of the structure and dynamics of E2~Ub conjugates is required for further mechanistic understanding of Ub transfer reactions. Here we present characterization of the dynamic behavior of E2~Ub conjugates of two human enzymes, UbcH5c~Ub and Ubc13~Ub,more » in solution as determined by nuclear magnetic resonance and small-angle X-ray scattering. Within each conjugate, Ub retains great flexibility with respect to the E2, indicative of highly dynamic species that adopt manifold orientations. The population distribution of Ub conformations is dictated by the identity of the E2: the UbcH5c~Ub conjugate populates an array of extended conformations, and the population of Ubc13~Ub conjugates favors a closed conformation in which the hydrophobic surface of Ub faces helix 2 of Ubc13. Finally, we propose that the varied conformations adopted by Ub represent available binding modes of the E2~Ub species and thus provide insight into the diverse E2~Ub protein interactome, particularly with regard to interaction with Ub ligases.« less