A protein residing at the subunit interface of the bacterial ribosome

AUTOR(ES)

Agafonov, Dmitry E.

FONTE

The National Academy of Sciences

RESUMO

Surface labeling of Escherichia coli ribosomes with the use of the tritium bombardment technique has revealed a minor unidentified ribosome-bound protein (spot Y) that is hidden in the 70S ribosome and becomes highly labeled on dissociation of the 70S ribosome into subunits. In the present work, the N-terminal sequence of the protein Y was determined and its gene was identified as yfia, an ORF located upstream the phe operon of E. coli. This 12.7-kDa protein was isolated and characterized. An affinity of the purified protein Y for the 30S subunit, but not for the 50S ribosomal subunit, was shown. The protein proved to be exposed on the surface of the 30S subunit. The attachment of the 50S subunit resulted in hiding the protein Y, thus suggesting the protein location at the subunit interface in the 70S ribosome. The protein was shown to stabilize ribosomes against dissociation. The possible role of the protein Y as ribosome association factor in translation is discussed.

Documentos Relacionados

• A charged residue at the subunit interface of PCNA promotes trimer formation by destabilizing alternate subunit interactions
• Packing at the protein-water interface.
• Bacterial microleakage at the implant-abutment interface in Morse taper implants
• Energy-driven subunit rotation at the interface between subunit a and the c oligomer in the FO sector of Escherichia coli ATP synthase
• Maize chloroplast DNA encodes a protein sequence homologous to the bacterial ribosome assembly protein S4.