Featured
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Letter |
Ubiquitin chain conformation regulates recognition and activity of interacting proteins
Single-molecule FRET assays used to probe the conformational dynamics of ubiquitin chains reveal that conformational selection is an important mechanism of ubiquitin chain recognition.
- Yu Ye
- , Georg Blaser
- & David Komander
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News & Views |
A protein engagement RING
The mechanistic details of the attachment of a small protein, ubiquitin, to other proteins are unclear. Crystal structures of the complexes formed by the E2–ubiquitin and RING E3 enzymes offer new insights. See Article p.115
- Christopher D. Lima
- & Brenda A. Schulman
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Article |
Recognition of SUMO-modified PCNA requires tandem receptor motifs in Srs2
Two carboxy-terminal motifs are necessary for Srs2 to recognize SUMO-conjugated PCNA, which is involved in DNA replication and repair; one motif is specific to SUMO, the other to PCNA.
- Anthony A. Armstrong
- , Firaz Mohideen
- & Christopher D. Lima
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Letter |
Cysteine methylation disrupts ubiquitin-chain sensing in NF-κB activation
A conserved protein from enteropathogenic Escherichia coli, NleE, inhibits innate immune defence against infection by disrupting the NF-κB signalling pathway through methylation of ubiquitin-chain sensing proteins.
- Li Zhang
- , Xiaojun Ding
- & Feng Shao
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Outlook |
On the wings of imagination
Biochemist at Technion, the Israeli Institute of Technology in Haifa. Shared the 2004 Nobel Prize in Chemistry for the discovery of the ubiquitin system, which mediates protein degradation in all plant and animal cells by destroying proteins that are denatured, misfolded or no longer needed. Family moved from Poland in the 1920s, and he was born in Haifa in 1947. The following year the state of Israel was established.
- Aaron Ciechanover
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Article |
Role of the ubiquitin-like protein Hub1 in splice-site usage and alternative splicing
- Shravan Kumar Mishra
- , Tim Ammon
- & Stefan Jentsch
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News & Views |
Transformative encounters
Researchers have met the challenge of capturing transient states of the SUMO E1 activating enzyme. Their pictures show radically different crystal structures for two of the steps in this enzyme's activity.
- Brenda A. Schulman
- & Arthur L. Haas
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Article |
Ubiquitin-like small archaeal modifier proteins (SAMPs) in Haloferax volcanii
Although Archaea encode proteasomes highly related to those of eukaryotes, archaeal ubiquitin-like proteins are less conserved and not known to function in protein conjugation, complicating our understanding of the origins of ubiquitination. Two small archaeal modifier proteins, SAMP1 and SAMP2, structurally similar to ubiquitin, are now reported to form protein conjugates in the archaeon Haloferax volcanii.
- Matthew A. Humbard
- , Hugo V. Miranda
- & Julie A. Maupin-Furlow
Capturing a substrate in an activated RING E3/E2–SUMO complex