Subcellular Protein Localization Event

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A Subcellular Protein Localization Event is a biological event where a subcellular protein becomes localized in a subcellular component.



References

2014

  1. Schuler D. (2004). Molecular analysis of a subcellular compartment: the magnetosome membrane in Magnetospirillum gryphiswaldense. Arch Microbiol. 181:1-7

2010

2007

2003

1993

  • (Pan, Trevor et al., 1993) ⇒ Shen Q. Pan, Trevor Charles, Shouguang Jin, Zhi-Liang Wu, and Eugene W. Nester. (1993). “Preformed dimeric state of the sensor protein VirA is involved in plant--Agrobacterium signal transduction.” In: Proceedings of the National Academy of Sciences, 90(21).
    • ABSTRACT: Plant signal molecules such as acetosyringone and certain monosaccharides induce the expression of Agrobacterium tumefaciens virulence (vir) genes, which are required for the processing, transfer, and possibly integration of a piece of the bacterial plasmid DNA (T-DNA) into the plant genome. Two of the vir genes, virA and virG, belonging to the bacterial two-component regulatory system family, control the induction of vir genes by plant signals. virA encodes a membrane-bound sensor kinase protein and virG encodes a cytoplasmic regulator protein. Although it is well established from in vitro studies that the signal transduction process involves VirA autophosphorylation and subsequent phosphate transfer to VirG, the structural state of the VirA protein involved in signal transduction is not understood. In this communication, we describe an in vivo crosslinking approach which provides physical evidence that VirA exists as a homodimer in its native configuration. The dimerization of VirA neither requires nor is stimulated by the plant signal molecule acetosyringone. We also present genetic data which support the hypothesis that VirA exists as a homodimer which is the functional state transducing the plant signal in an intersubunit mechanism. To our knowledge, this report provides the first evidence that a bacterial membrane-bound sensor kinase exists and functions as a homodimer in vivo.