This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Casjens, S Articles by King, J Search for Related Content PubMed PubMed Citation Articles by Casjens, S Articles by King, J

 Previous Article  |  Next Article 

J Virol. 1985 January; 53(1): 174-179

Assembly-controlled autogenous modulation of bacteriophage P22 scaffolding protein gene expression.

ABSTRACT

In the assembly of bacteriophage P22, precursor particles containing two major proteins, the gene 5 coat protein and the gene 8 scaffolding protein, package the DNA molecule. During the encapsidation reaction all of the scaffolding protein molecules are released intact and subsequently participate in further rounds of DNA encapsidation. We have previously shown that even though it lies in the center of the late region of the genetic map, the scaffolding protein gene is not always expressed coordinately with the remainder of the late proteins and that some feature of the phage assembly process affects its expression. We present here in vivo experiments which show that there is an inverse correlation between the amount of unassembled scaffolding protein and the rate of scaffolding protein synthesis and that long amber fragments of the scaffolding protein can turn down the synthesis of intact scaffolding protein in trans. These results support a model for scaffolding protein regulation in which the feature of the assembly process which modulates the rate of scaffolding protein synthesis is the amount of unassembled scaffolding protein itself.

This article has been cited by other articles:

• Greene, B., King, J. (1999). In Vitro Unfolding/Refolding of Wild Type Phage P22 Scaffolding Protein Reveals Capsid-binding Domain. J. Biol. Chem. 274: 16135-16140 [Abstract] [Full Text]  
• Yamanaka, G., DiIanni, C. L., O'Boyle, D. R. II, Stevens, J., Weinheimer, S. P., Deckman, I. C., Matusick-Kumar, L., Colonno, R. J. (1995). Stimulation of the Herpes Simplex Virus Type I Protease by Antichaeotrophic Salts. J. Biol. Chem. 270: 30168-30172 [Abstract] [Full Text]