Eric C. Becker
University of California, San Diego
21 Papers
202 Citations
Eric C. Becker is an academic researcher from University of California, San Diego. The author has contributed to research in topics: Origin of transfer & Plasmid. The author has an hindex of 16, co-authored 21 publications. Previous affiliations of Eric C. Becker include University of Texas at Austin.
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Papers
Bacillus subtilis MinC destabilizes FtsZ-rings at new cell poles and contributes to the timing of cell division
TL;DR: These results suggest that B. subtilis MinC prevents polar FtsZ rings adjacent to new cell poles from supporting cell division, rather than mediating the stable polar localization previously thought to restrict MinC activity to the pole.
Phylogenetic analysis identifies many uncharacterized actin-like proteins (Alps) in bacteria: regulated polymerization, dynamic instability and treadmilling in Alp7A.
Alan I. Derman,Eric C. Becker,Bao D. Truong,Akina Fujioka,Timothy M. Tucey,Marcella L. Erb,Paula C. Patterson,Joe Pogliano +7 more
TL;DR: A phylogenetic search is conducted and it is suggested that most if not all of the Alps are indeed actin relatives, and that actin is very well represented in bacteria.
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DNA segregation by the bacterial actin AlfA during Bacillus subtilis growth and development.
Eric C. Becker,Nick C Herrera,Felizza F. Gunderson,Alan I. Derman,Amber L. Dance,Jennifer Sims,Rachel A. Larsen,Joe Pogliano +7 more
TL;DR: A protein (AlfA; actin like filament) is identified that defines a new family of actins that are only distantly related to MreB and ParM, and the dynamic polymerization of AlfA mediates plasmid separation during both growth and sporulation.
Flk prevents premature secretion of the anti‐σ factor FlgM into the periplasm
Phillip D. Aldridge,Joyce E. Karlinsey,Eric C. Becker,Fabienne F. V. Chevance,Kelly T. Hughes +4 more
TL;DR: Evidence is presented which suggests that Flk is a cytoplasmic‐facing protein anchored to the inner membrane by a single, C‐terminal transmembrane‐spanning domain (TMS) that is not essential for Flk activity, but membrane anchoring is essential.