# ANTIBIOTIC PROBES OF RIBOSOMAL STRUCTURE AND FUNCTION

> **NIH NIH R01** · UNIVERSITY OF PENNSYLVANIA · 1989 · $176,435

## Abstract

Our overall goal in this work is to obtain a detailed description of the E.
coli ribosomal binding sites of antibiotics and other ribosomal ligands of
known function.  Taken together with ongoing efforts in several
laboratories directed toward obtaining a topographic map of the ribosome,
such a description should provide the basis for a detailed understanding of
the inhibitory effects of antibiotics on protein synthesis, as well as
contribute to a better understanding of the relationship between ribosome
structure and function.  Such improved understanding could well lead to the
development of improved antibiotics for therapeutic use.

Our approach makes use of the techniques of affinity labeling, DNA.RNA
hybridization, immunoelectron microscopy, reconstitution, and HPLC to
characterize the sites and functional significance of antibiotic and
rellated ligand binding to the ribosome.  For the coming grant period, our
immediate goals are:

1. To Map Protein at Sites of or Related to Antibiotic Binding.  We will
identify proteins into which antibiotic affinity labels incorporate and
determine the specificity of such incorporation.  Proteins prepared by HPLC
will be used to reconstitute ribosomal subunits in which a single,
affinity-labeled protein replaces its corresponding native protein and all
other proteins are added as native proteins.  Functional tests on such
subunits should provide important evidence for placing particular proteins
at an antibiotic binding site.  Such subunits will also be used for
immunoelectron microscopy experiments, allowing three-dimensional
localization not only of the antibiotic but also of the protein into which
it is incorporated.

2. Localize Site of Affinity Labeling of Ribosomal RNA.  We will further
improve our RNA DNA hybridization method for localizing sites of labeling
in RNA, and extend such localization to the oligonucleotide level.

3. Synthesize and Test Other Antibiotic Affinity Labels.  We plan a
vigorous program of synthesis of radioactive affinity labels, both
photolabile and electrophilic, to extend our work to antibiotics other than
those (puromycin, tetracycline, and streptomycin) we have emphasized until
now.  These include:  lincomycin, chloramphenicol, tiamulin, and tobramycin.

## Key facts

- **NIH application ID:** 3126862
- **Project number:** 5R01AI016806-10
- **Recipient organization:** UNIVERSITY OF PENNSYLVANIA
- **SAM.gov UEI:** GM1XX56LEP58
- **Principal Investigator:** BARRY S. COOPERMAN
- **Activity code:** R01 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 1989
- **Award amount:** $176,435
- **Award type:** 5
- **Project period:** 1980-06-01 → 1990-08-31

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/3126862

## Citation

> US National Institutes of Health, RePORTER application 3126862, ANTIBIOTIC PROBES OF RIBOSOMAL STRUCTURE AND FUNCTION (5R01AI016806-10). Retrieved via MORVS 2026-10-25 from https://api.morvs.ai/grant/nih/3126862. Licensed CC0.

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