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Homodimerization of Tsi2 is not critical for Tse2–Tsi2 interaction.

By Mo Li (43239), Isolde Le Trong (171802), Mike A. Carl (171808), Eric T. Larson (171813), Seemay Chou (171820), Justin A. De Leon (171825), Simon L. Dove (171833), Ronald E. Stenkamp (171836) and Joseph D. Mougous (171842)

Abstract

<p>(A) Ribbon representation of the Tsi2 dimer interface. Amino acids positions substituted non-conservatively to disrupt the dimer interface are labeled on monomer A and shown in stick representation. (B) Top – B2H analysis of homodimerization of the indicated Tsi2 dimer interface substitution variants. Genes fused in-frame to RNAP–ω and Zif are indicated. Bottom – Western blot analysis of the expression of <i>tsi2–V–zif</i> alleles within the indicated strains. (C) Western blot analysis of Tsi2–biotin–maleimide conjugates. Equal concentration of purified Tsi2 variants (10 µM) were reacted for the indicated time periods with 10 µM of a biotin-maleimide conjugate. (D) B2H analysis of the interaction between wild-type Tsi2 and Tsi2<sup>A47Q</sup> with Tse2. Genes fused in-frame to RNAP–ω and Zif are indicated. (E) Growth of <i>E. coli</i> stains expressing <i>tse2</i> alone, or co-expressing <i>tse2</i> with the indicated allele of <i>tsi2</i>, under non-inducing (−IPTG) or inducing (+IPTG) conditions.</p

Topics: Biochemistry, Microbiology, tsi2
Year: 2012
DOI identifier: 10.1371/journal.ppat.1002613.g006
OAI identifier: oai:figshare.com:article/325870
Provided by: FigShare
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