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Is TALL-1 a trimer or a virus-like cluster?

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Abstract

Native TALL-1 (B-cell activation factor, BAFF; also known as BlyS) was initially described as a homotrimer1,2,3, but Liu and colleagues claim that it is a 60-subunit complex4,5,6 on the basis of their results from X-ray crystallography and size-exclusion chromatography. They consider TALL-1 60-mers to be the biologically active form, and the arrangement of the 60-mers resembles that of the capsid of satellite tobacco necrosis virus4,5,6. Here we show that active TALL-1 is trimeric under normal physiological conditions and that formation of higher-order oligomers is an artefact of tagging the amino terminus of the protein with a histidine tag.

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Figure 1: Effect of different amino-terminal tags on the oligomerization and biological properties of TALL-1.

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Authors and Affiliations

  1. Xencor, Monrovia, 91016, California, USA

    Eugene A. Zhukovsky, Michael Villegas, Cheryl Chan, Seung Chu & Cameron Mroske

  2. Department of Chemistry and School of Molecular Science, KAIST, Daejeon, 305–701, Korea

    Jie-Oh Lee

Authors
  1. Eugene A. Zhukovsky
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  2. Jie-Oh Lee
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  3. Michael Villegas
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  4. Cheryl Chan
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  5. Seung Chu
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  6. Cameron Mroske
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Corresponding author

Correspondence to Eugene A. Zhukovsky.

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Zhukovsky, E., Lee, JO., Villegas, M. et al. Is TALL-1 a trimer or a virus-like cluster?. Nature 427, 413–414 (2004). https://doi.org/10.1038/427413a

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