Abstract:
:For the study of the protein--protein and protein--nucleic acid interactions in the assembly of virus particles, laser Raman spectra have been obtained in H2O and D2O solutions and as a function of temperature for the following Salmonella phage P22 components: mature phage particles, isolated mature phage DNA, mature protein shells empty of DNA, precursor protein shells (procapsids), and purified coat, scaffolding and tail-spike proteins. The spectra confirm that the condensed DNA within the phage capsid assumes the B-form secondary structure similar to aqueous DNA and reveal no evidence of specific molecular interactions between subgroups of DNA and protein subunits of the phage capsid. No differences were detected in the highly irregular secondary structure of the major capsid protein in mature capsids, empty capsids (lacking DNA), procapsids, and empty procapsids (lacking scaffolding protein). Features of both primary and secondary structures of the viral scaffolding and tail-spike proteins are also revealed by the spectra. Differences in thermal stability of tyrosyl side-chain interactions were observed between scaffolding protein extracted from the procapsid and within the procapsid. These differences correspond to different hydrogen bonding configurations of p-hydroxyphenyl groups and provide indirect evidence for the participation of the scaffolding proteins in specific macromolecular interactions within the procapsid.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Thomas GJ Jr,Li Y,Fuller MT,King Jdoi
10.1021/bi00259a023subject
Has Abstractpub_date
1982-08-03 00:00:00pages
3866-78issue
16eissn
0006-2960issn
1520-4995journal_volume
21pub_type
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