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Sequence context and crosslinking mechanism affect the efficiency of in vivo capture of a protein–protein interaction

dc.contributor.authorLancia, Jody K.en_US
dc.contributor.authorNwokoye, Adaoraen_US
dc.contributor.authorDugan, Amandaen_US
dc.contributor.authorJoiner, Cassandraen_US
dc.contributor.authorPricer, Rachelen_US
dc.contributor.authorMapp, Anna K.en_US
dc.contributor.authorBreslauer, Kenneth J.en_US
dc.date.accessioned2014-02-11T17:57:06Z
dc.date.available2015-06-01T15:48:44Zen_US
dc.date.issued2014-04en_US
dc.identifier.citationLancia, Jody K.; Nwokoye, Adaora; Dugan, Amanda; Joiner, Cassandra; Pricer, Rachel; Mapp, Anna K.; Breslauer, Kenneth J. (2014). "Sequence context and crosslinking mechanism affect the efficiency of in vivo capture of a protein–protein interaction." Biopolymers 101(4): 391-397.en_US
dc.identifier.issn0006-3525en_US
dc.identifier.issn1097-0282en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/102672
dc.description.abstractProtein–protein interactions (PPIs) are essential for implementing cellular processes and thus methods for the discovery and study of PPIs are highly desirable. An emerging method for capturing PPIs in their native cellular environment is in vivo covalent chemical capture, a method that uses nonsense suppression to site specifically incorporate photoactivable unnatural amino acids (UAAs) in living cells. However, in one study we found that this method did not capture a PPI for which there was abundant functional evidence, a complex formed between the transcriptional activator Gal4 and its repressor protein Gal80. Here we describe the factors that influence the success of covalent chemical capture and show that the innate reactivity of the two UAAs utilized, ( p‐ benzoylphenylalanine (pBpa) and p ‐azidophenylalanine (pAzpa)), plays a profound role in the capture of Gal80 by Gal4. Based upon these data, guidelines are outlined for the successful use of in vivo photo‐crosslinking to capture novel PPIs and to characterize the interfaces. © 2013 Wiley Periodicals, Inc. Biopolymers 101: 391–397, 2014.en_US
dc.publisherWiley Periodicals, Inc.en_US
dc.subject.otherCrosslinkingen_US
dc.subject.otherGal80en_US
dc.subject.otherGal4en_US
dc.subject.otherUnnatural Amino Aciden_US
dc.subject.otherProtein–Protein Interactionsen_US
dc.titleSequence context and crosslinking mechanism affect the efficiency of in vivo capture of a protein–protein interactionen_US
dc.typeArticleen_US
dc.rights.robotsIndexNoFollowen_US
dc.subject.hlbsecondlevelChemistryen_US
dc.subject.hlbsecondlevelMaterials Science and Engineeringen_US
dc.subject.hlbsecondlevelChemical Engineeringen_US
dc.subject.hlbtoplevelEngineeringen_US
dc.subject.hlbtoplevelScienceen_US
dc.description.peerreviewedPeer Revieweden_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/102672/1/bip22395.pdf
dc.identifier.doi10.1002/bip.22395en_US
dc.identifier.sourceBiopolymersen_US
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dc.owningcollnameInterdisciplinary and Peer-Reviewed


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