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Nucleic Acids Research, 1993, Vol. 21, No. 3 635-639
© 1993

MOLECULAR BIOLOGY

Erythromycin and 5S rRNA binding properties of the spinach chloroplast ribosomal protein CL22

Pierre Carol, Claude Rozier, Ester Lazaro1, Juan P.G. Ballesta1 and Régis Mache*

Laboratoire de Biologie Moléculaire Végétale U.J.Fourier BP 53X, 38041 Grenoble Cedex, France 1Centro de Biologia Molecular ‘Severo Ochoa’ (CSIC-UAM) Canto Blanco, 28049 Madrid, Spain

*To whom correspondence should be addressed

Received September 25, 1992. Revised December 18, 1992. Accepted December 18, 1992.

The spinach chloropiast ribosomal protein (r-protein) CL22 contains a central region homologous to the Escherichia coli r-protein L22 pius long N- and C-terminal extensions. We show in this study that the CL22 combines two properties which in E.coli ribosome are split between two separate proteins. The CL22 which binds to the 5S rRNA can also be linked to an erythromycin derivative added to the 50S ribosomal subunit. This latter property is similar to that of the E.coli L22 and suggests a similar localization in the 50S subunit. We have overproduced the r-protein CL22 and deleted forms of this protein in E.coli. We show that the overproduced CL22 binds to the chioroplast 5S rRNA and that the deleted protein containing the N- and C-terminal extensions only has lost the 5S rRNA binding property. We suggest that the central homologous regions of the CL22 contains the RNA binding domain.


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