Electron microscopy of bacillus subtilis groesl chaperonin and interaction with the bacteriophage φ29 head-tail connector

Vladimir Tsuprun, Basavapatna S. Rajagopal, Dwight Anderson

Research output: Contribution to journalArticlepeer-review

4 Scopus citations

Abstract

The Bacillus subtilis GroESL chaperonin was isolated by sucrose density gradient centrifugation and the constituent GroES and GroEL moieties were purified by electrophoresis in agarose. Electron microscopic images of negatively stained GroEL and GroES oligomers and GroESL complexes were averaged using a reference-free alignment method. The GroEL and GroES particles had the sevenfold symmetry characteristic of their Escherichia coli counterparts. GroESL complexes, reconstituted efficiently in vitro from GroEL and GroES in the absence of added ADP or ATP, had the characteristic bullet- and football-like shapes in side view. Purified bacteriophage φ29 head-tail connectors having a mass in excess of 0.4 MDa were shown to bind to GroESL at the end opposite to the GroES. The same GroESL-connector complexes were isolated from phage-infected cells in which capsid assembly was blocked, and thus the complex may have functional significance in φ29 morphogenesis.

Original languageEnglish (US)
Pages (from-to)258-266
Number of pages9
JournalJournal of Structural Biology
Volume115
Issue number3
DOIs
StatePublished - Nov 1995

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