Deletion analysis and alanine-scanning based on a homology-based interaction model were used to identify determinants of oligomerization in the transcriptional regulator CynR, a member of the LysR-type transcriptional regulator (LTTR) family. Deletion analysis confirmed that the putative regulatory domain of CynR was essential for driving the oligomerization of lambda repressor-CynR fusion proteins. The interaction surface of a different LTTR and OxyR was mapped onto a multiple sequence alignment of the LTTR family. This mapping identified putative contacts in the CynR regulatory domain dimer interface, which were targeted for alanine-scanning mutagenesis. Oligomerization was assayed by the ability of mutant lambda repressor-CynR fusions to assemble in E. coli revealing interesting similarities and differences between OxyR and CynR.
Protein science : a publication of the Protein Society. 2009 Nov;18(11):2307-15. doi: 10.1002/pro.241 Q15.22025
The oligomerization of CynR in Escherichia coli
大肠杆菌中CynR的寡聚化 翻译改进
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DOI: 10.1002/pro.241 PMID: 19760662
摘要 Ai翻译
Keywords：CynR oligomerization; Escherichia coli
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