Abstract
Protein interactions in the assembly of the baseplate have been investigated. The baseplate of the phage T4 tail consists of a hub and six wedges which surround the former. Both reversible and irreversible interactions were found. Reversible association includes gp5 and gp27 (gp: gene product) which form a complex in a pH-dependent manner and gp18 polymerization, i.e. the tail sheath formation depends on the ionic strength. These reversible interactions were followed by irreversible or tight binding which pulls the whole association reaction to complete the assembly. The wedge assembly is strictly ordered which means that if one of the seven wedge proteins is missing, the assembly proceeds to that point and the remaining molecules stay non-associated. The strictly sequential assembly pathway is suggested to be materialized by successive conformational change upon binding, which can be shown by proteolytic probe.
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Acknowledgements
I first encountered Dr. Minton in the early summer of 1997 when I sent a question of mine to RASMB internet forum. I cannot recall what it was, but he kindly replied to my question and we started to exchange e-mails. I thought he was in the U.S.A., but actually he was at that time staying at Protein Research Institute of Osaka University. So, I invited him to give a seminar at our institute. The next year, I went to Melbourne to attend the Lorne Conference and its satellite meeting on Reversible Associations in Structural and Molecular Biology which was held at the university of Melbourne prior to the Lorne meeting. I saw him there again. Three years later in 2001, I had an opportunity to organize a small international conference in the framework of Keihanna International Conference on Molecular Biophysics and invited Allen as a guest speaker. In 2003, my proposal to invite him for three months as a visiting professor was accepted by our Graduate School. It was a very stimulating experience for me to talk daily to him. He came to Japan again in 2006 as a JSPS fellow for short term research communication, where he constructed a hand-made CG machine to attach to our light scattering machine. That was before commercial CG instrument, Calypso, was available. At the time of writing this article, Dr. Minton is visiting our laboratory for collaboration together with Dr. Damien Hall from the University of Tsukuba. I greatly appreciate his ever-lasting stimulating enthusiasm, discussion and encouragement.
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Special Issue: Protein–Protein and Protein–Ligand Interactions in Dilute and Crowded Solution Conditions. In Honor of Allen Minton’s 70th Birthday
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Arisaka, F., Kanamaru, S. Protein interactions in the assembly of the tail of bacteriophage T4. Biophys Rev 5, 79–84 (2013). https://doi.org/10.1007/s12551-013-0114-2
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DOI: https://doi.org/10.1007/s12551-013-0114-2