Conformational flexibility of a ubiquitin conjugation enzyme (E2)

Qin Liu, Yate Ching Yuan, Binghui Shen, David J. Chen, Yuan Chen

Research output: Contribution to journalArticle

27 Citations (Scopus)

Abstract

Ubiquitination plays important roles in a variety of biological processes, such as DNA repair, cell cycle regulation, and p53-dependent processes. Despite intensive studies in ubiquitination, the mechanism of substrate recognition is still not well understood. Each E2 has its own substrate specificity, yet substrate proteins recognized by each E2 are highly diverse. To better understand how E2 proteins confer both substrate specificity and diversity, we have studied conformational flexibility of an E2, UBC9, using nuclear magnetic resonance 15N relaxation and hydrogen- deuterium exchange measurements. Two regions in human UBC9 show higher mobility over a wide range of time scales. Combined with previous biochemical studies, both regions are likely to be important for protein-protein recognition in the ubiquitin pathway. The region near the N-terminus may be important for interactions with the E1-UBL1 conjugate. The region near the C- terminus, which undergoes conformational exchange may be important for substrate binding and catalytic activity. Since E2 enzymes share high homology in primary sequences and three-dimensional structures, the conformational flexibility of UBC9 may represent a general feature of E2 enzymes. This study provides a new perspective for further studies of protein-protein recognition in ubiquitination.

Original languageEnglish (US)
Pages (from-to)1415-1425
Number of pages11
JournalBiochemistry
Volume38
Issue number5
DOIs
StatePublished - Feb 2 1999

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Ubiquitin
Ubiquitination
Enzymes
Substrates
Proteins
Substrate Specificity
Deuterium Exchange Measurement
Biological Phenomena
Deuterium
DNA Repair
Hydrogen
Catalyst activity
Cell Cycle
Repair
Magnetic Resonance Spectroscopy
Cells
Nuclear magnetic resonance
DNA

ASJC Scopus subject areas

  • Biochemistry

Cite this

Conformational flexibility of a ubiquitin conjugation enzyme (E2). / Liu, Qin; Yuan, Yate Ching; Shen, Binghui; Chen, David J.; Chen, Yuan.

In: Biochemistry, Vol. 38, No. 5, 02.02.1999, p. 1415-1425.

Research output: Contribution to journalArticle

Liu, Qin ; Yuan, Yate Ching ; Shen, Binghui ; Chen, David J. ; Chen, Yuan. / Conformational flexibility of a ubiquitin conjugation enzyme (E2). In: Biochemistry. 1999 ; Vol. 38, No. 5. pp. 1415-1425.
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