Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/39052
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Título : Importance of the N-terminal Region of the Phage GA-1 Single-stranded DNA-binding Protein for Its Self-interaction Ability and Functionality
Autor : Gascón, Irene, Carrascosa, José L., Villar, Laurentino, Lázaro, José M., Salas, Margarita
Fecha de publicación : 15-Apr-2002
Editor: American Society for Biochemistry and Molecular Biology
Citación : Journal of Biological Chemistry 277: 22534-22540 (2002)
Resumen: The single-stranded DNA-binding protein (SSB) of phage GA-1 displays higher efficiency than the SSBs of the related phages φ29 and Nf. In this work, the self-interaction ability of GA-1 SSB has been analyzed by visualization of the purified protein by electron microscopy, glycerol gradient sedimentation, and in vivo cross-linking of bacterial cultures infected with phage GA-1. GA-1 SSB contains an insert at its N-terminal region that is not present in the SSBs of φ29 and Nf. Three deletion mutant proteins have been characterized, ΔN19, ΔN26, and ΔN33, which lack the 19, 26 or 33 amino acids, respectively, that follow the initial methionine of GA-1 SSB. Mutant protein ΔN19 retains the structural and functional behavior of GA-1 SSB, whereas mutant proteins ΔN26 and ΔN33 no longer stimulate viral DNA replication or display helix-destabilizing activity. Analysis of the mutant proteins by ultracentrifugation in glycerol gradients and electron microscopy indicates that deletion of 26 or 33 but not of 19 amino acids of the N-terminal region of GA-1 SSB results in the loss of the oligomerization ability of this protein. Our data support the importance of the N-terminal region of GA-1 SSB for the differential self-interaction ability and functional behavior of this protein.
Versión del editor: http://dx.doi.org/10.1111/j.1432-1033.1977.tb11291.x
URI : http://hdl.handle.net/10261/39052
ISSN: 0021-9258
DOI: 10.1074/jbc.M202430200
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