Properties of the Major Nucleocapsid Protein of Heliothis zea Singly Enveloped Nuclear Polyhedrosis Virus

Autor:	I. O. Walker, D. A. Brown, Cynthia J. Allen, D. C. Kelly, M. D. Ayres
Rok vydání:	1983
Předmět:	Conformational change biology viruses Lysine Spodoptera litura Nuclear Polyhedrosis Virus biology.organism_classification Virology DNA-binding protein Virus Capsid Biochemistry Trichoplusia
Zdroj:	Journal of General Virology. 64:399-408
ISSN:	1465-2099 0022-1317
DOI:	10.1099/0022-1317-64-2-399
Popis:	Summary The major nucleocapsid protein of Heliothis zea single nucleocapsid nuclear polyhedrosis virus is a low mol. wt., basic, DNA-binding protein present in the core of the capsid. It is rich in arginine and helix-destabilizing residues and possesses no lysine nor hydrophobic residues. Circular dichroism analysis showed that the protein undergoes a major conformational change in high salt solutions involving the tyrosine side chains. There is sufficient of this protein in the nucleocapsid for all the genome phosphate to be neutralized by arginine residues. A comparison of the protein with similar basic proteins from Spodoptera litura granulosis virus, Oryctes rhinoceros non-occluded baculovirus, and Trichoplusia ni multiple nucleocapsid nuclear polyhedrosis virus showed that they are all arginine-rich, lysine-poor, DNA-binding proteins.
Databáze:	OpenAIRE
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