Selected article for: "amino acid and cellular protein"
Author: Megan C. Cohan; Ammon E. Posey; Steven J. Grigsby; Anuradha Mittal; Alex S. Holehouse; Paul J. Buske; Petra A. Levin; Rohit V. Pappu
Title: Evolved sequence features within the intrinsically disordered tail influence FtsZ assembly and bacterial cell division
  • Document date: 2018_4_14
    • ID: 2rzfuy33_73
    Snippet: Our findings suggest that the CTT / CTL encoded effects cannot be too weak (low κ) or too strong (κ > 0.4); instead, they have to be just right because the CTT plays multiple regulatory roles. In addition, the sequence complexity of the CTT also has to be above a threshold value to ensure protein stability in the cellular setting. We refer to this combination of requirements as a "Goldilocks precept" for the evolution of sequence features withi.....
    Document: Our findings suggest that the CTT / CTL encoded effects cannot be too weak (low κ) or too strong (κ > 0.4); instead, they have to be just right because the CTT plays multiple regulatory roles. In addition, the sequence complexity of the CTT also has to be above a threshold value to ensure protein stability in the cellular setting. We refer to this combination of requirements as a "Goldilocks precept" for the evolution of sequence features within IDPs / IDRs. Similar results have been uncovered from a deep mutational scan of the transactivation domain of Gcn4, which is an essential transcription factor in yeast (Staller et al., 2018) . Our investigations open the door for systematic high-throughput experiments guided by recent computational advances (Harmon et al., 2016) that enable the design of CTT sequences with bespoke sequence complexities, lengths, amino acid compositions, and charge patterning.

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