The functions of the N terminus of the φX174 internal scaffolding protein, a protein encoded in an overlapping reading frame in a two scaffolding protein system

Christopher R. Novak, Bentley A Fane

Research output: Contribution to journalArticle

20 Citations (Scopus)

Abstract

φX174 utilizes two scaffolding proteins during morphogenesis, an internal protein (B) and an external protein (D). The B protein induces a conformational change in coat protein pentamers, enabling them to interact with both spike and external scaffolding proteins. While functions of the carboxyl terminus of protein B have been defined, the functions of the amino terminus remain obscure. To investigate the morphogenetic functions of the amino terminus, several 5′ deleted genes were constructed and the proteins expressed in vivo. The ΔNH2 B proteins were assayed for the ability to complement an ochre B mutant and defects in the morphogenetic pathway were characterized. The results of the biochemical, genetic and second-site genetic analyses indicate that the amino terminus induces conformational changes in the viral coat protein and facilitates minor spike protein incorporation. Defects in conformational switching can be suppressed by substitutions in the external scaffolding protein, suggesting some redundancy of function between the two proteins.

Original languageEnglish (US)
Pages (from-to)383-390
Number of pages8
JournalJournal of Molecular Biology
Volume335
Issue number1
DOIs
StatePublished - Jan 2 2004

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Reading Frames
Proteins
Capsid Proteins
Morphogenesis
Molecular Biology
IgA receptor
Genes

Keywords

  • φX174
  • Morphogenesis
  • Procapsid
  • Scaffolding protein

ASJC Scopus subject areas

  • Virology

Cite this

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