1. Novel DNA packaging recognition in the unusual bacteriophage N15
- Author
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Henriette Geyer, Jean Sippy, Franco Klingberg, Amanda Forystek, Nasib Karl Maluf, Norma Moreno, and Michael Feiss
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Virus DNA packaging ,Article ,Bacteriophage ,03 medical and health sciences ,Endonuclease ,chemistry.chemical_compound ,Virology ,Bacteriophages ,Binding site ,Prophage ,030304 developmental biology ,Genetics ,0303 health sciences ,Binding Sites ,Endodeoxyribonucleases ,biology ,DNA packaging ,030302 biochemistry & molecular biology ,food and beverages ,DNA-binding domain ,Lambda phage ,biology.organism_classification ,Virus evolution ,Virus assembly ,DNA binding site ,chemistry ,DNA, Viral ,Virus DNA recognition ,biology.protein ,Terminase ,DNA - Abstract
Phage lambda׳s cosB packaging recognition site is tripartite, consisting of 3 TerS binding sites, called R sequences. TerS binding to the critical R3 site positions the TerL endonuclease for nicking cosN to generate cohesive ends. The N15 cos (cosN15) is closely related to cosλ, but whereas the cosBN15 subsite has R3, it lacks the R2 and R1 sites and the IHF binding site of cosBλ. A bioinformatic study of N15-like phages indicates that cosBN15 also has an accessory, remote rR2 site, which is proposed to increase packaging efficiency, like R2 and R1 of lambda. N15 plus five prophages all have the rR2 sequence, which is located in the TerS-encoding 1 gene, approximately 200 bp distal to R3. An additional set of four highly related prophages, exemplified by Monarch, has R3 sequence, but also has R2 and R1 sequences characteristic of cosB–λ. The DNA binding domain of TerS-N15 is a dimer.
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