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Controlled enzymatic synthesis of natural-linkage, defined-length polyubiquitin chains using lysines with removable protecting groups.

ABSTRACT: E2 enzymes catalyze the ATP-dependent polymerization of polyubiquitin chains which function as molecular signals in the regulation of numerous cellular processes. Here we present a method that uses genetically encoded unnatural amino acids to halt and re-start ubiquitin polymerization providing access to natural-linkage, precision-length ubiquitin chains that can be used for biochemical, structural, and dynamics studies.

SUBMITTER: Castaneda CA

PROVIDER: S-EPMC3190230 | biostudies-literature | 2011 Feb

REPOSITORIES: biostudies-literature

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Controlled enzymatic synthesis of natural-linkage, defined-length polyubiquitin chains using lysines with removable protecting groups.

Castañeda Carlos A CA Liu Jia J Kashyap Tanuja R TR Singh Rajesh K RK Fushman David D Cropp T Ashton TA

Chemical communications (Cambridge, England) 20110106 7

E2 enzymes catalyze the ATP-dependent polymerization of polyubiquitin chains which function as molecular signals in the regulation of numerous cellular processes. Here we present a method that uses genetically encoded unnatural amino acids to halt and re-start ubiquitin polymerization providing access to natural-linkage, precision-length ubiquitin chains that can be used for biochemical, structural, and dynamics studies. ...[more]

PMID: 21212884

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