Segmental flexibility in Escherichia coli ribosomal protein S1 as studied by fluorescence polarization.

AUTOR(ES)

Chu, Y G

RESUMO

Ribosomal protein S1 covalently reacts with approximately one equivalent of iodoacetylethylenediamine (1,5-napthol sulfonate (IAEDANS) or iodoacetylaminofluorescein (IAAF). The product AEDANS-S1 can bind to 30S ribosomal subunits lacking S1 as shown by polyacrylamide-agarose gel electrophoresis AEDANS-S1 and AAF-S1 when added back to S1-depleted 30S subunits modulate poly(U)-dependent polyphenylalanine synthesis in the presence of IF3 in a very similar way to unmodified S1. AEDANS-S1 also stimulates RI7-dependent fMet-tRNA binding to 1.0M NH4C1 washed ribosomes whereas AAF-S1 does not. Both static and nanosecond fluorescence polarization techniques were used to study the rotational motions of AEDANS-S1. Several previous studies had indicated that S1 is a highly extended protein which can be modeled by a prolate ellipsoid with an axial ratio of 10 to 1. However, the rotational correlation time we find is about half that expected for such a particle. This suggests that S1 is a flexible protein with at least two domains that can rotate independently.

Documentos Relacionados

• Interaction of Escherichia coli ribosomal protein S1 with ribosomes.
• Escherichia coli ribosomal protein S1 has two polynucleotide binding sites.
• Primary structure of Escherichia coli ribosomal protein S1 and of its gene rpsA.
• Specific Binding of Escherichia coli Ribosomal Protein S1 to boxA Transcriptional Antiterminator RNA
• Levels of ribosomal protein S1 and elongation factor G in the growth cycle of Escherichia coli.