Abstract
The repressor gene from the Streptomyces phage φC31 expresses three N-terminally different, in-frame protein isoforms of polypeptide molecular masses 74, 54 and 42 kDa. Their precise role in the lysis versus lysogeny decision is currently being investigated and a study of their structural and interactive properties was considered an important aid in this investigation. The preliminary data presented here shows that the native 42 kDa isoform and a Histidine (His-)-tagged form exist as dimers or tetramers, depending on the conditions as determined by sedimentation equilibrium in the analytical ultracentrifuge.
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References
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© 1995 Dr. Dietrich Steinkopff Verlag GmbH & Co. KG
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Jumel, K., Wilson, S.E., Smith, M.C.M., Harding, S.E. (1995). Investigations of the oligometric state of the 42 kDa repressor isoform from the streptomcyes temperate bacteriophage φC31. In: Behlke, J. (eds) Analytical Ultracentrifugation. Progress in Colloid & Polymer Science, vol 99. Steinkopff. https://doi.org/10.1007/BFb0114064
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DOI: https://doi.org/10.1007/BFb0114064
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