Abstract
The ribosome is a ribonucleoprotein particle composed of two unequal subunits. Correct association of the two subunits is required for proper ribosome function. X‐ray crystal structures of fully assembled bacterial ribosomes have identified a number of specific interactions, or intersubunit bridges (ISBs), between the large (60S) and small (40S) subunits. Modification interference studies have shown that at least two of these ISBs are important for ribosome stability in bacteria. We are using a similar modification interference approach to identify ISBs that are important for ribosome stability in yeast. To date we have performed sucrose gradient ultracentrifugation under a variety of conditions to dissociate ribosomal subunits from intact 80S ribosomes. Chemical modifications of the purified 40S subunits are currently underway. Subsequently, modified 40S subunits will be allowed to reassociate with native 60S subunits. Presumably, those 40S subunits that are unable to stably reassociate will have been modified at RNA bases involved in important ISBs. We hope these studies will provide insights regarding the function and conservation of ISBs. Supported by the Dreyfus Foundation and the Jeffress Memorial Trust.
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