# Investigating the structure, function, and regulation of polyamine acetyltransferases

> **NIH NIH R35** · SAN FRANCISCO STATE UNIVERSITY · 2020 · $171,005

## Abstract

PROJECT SUMMARY
The proposed research seeks to study the functions and regulation of bacterial polyamine acetyltransferases
(PAATs). These enzymes belong to the large Gcn5-related N-acetyltransferase (GNAT) superfamily, and
acetylate a variety of polyamines including spermine, spermidine, and norspermidine. The main function
associated with bacterial PAATs has been to maintain intracellular polyamine concentrations; however,
increasing evidence has shown that PAATs likely play a larger role in bacterial physiology and pathogenesis
than previously anticipated. While PAATs have been well-studied in eukaryotes, there is a significant gap in
knowledge regarding bacterial PAAT identities, functions and regulation. Additionally, there is a limited
understanding of how allosteric effectors and oligomerization regulate PAAT function, and how these properties
effect PAAT roles in bacterial biofilms and other cellular processes. Since polyamines have been implicated in
bacterial virulence and pathogenesis, knowledge about PAAT regulation is critical for developing effective
therapeutics toward bacterial pathogens. Therefore, the goal of the proposed research is to determine the roles
of PAATs and how they are regulated across pathogenic and non-pathogenic bacteria. We will investigate the
following key questions over the next five years: 1) Which bacterial GNATs are PAATs?, 2) How are bacterial
PAATs regulated?, and 3) How do bacterial PAATs regulate cellular processes?. The answers to these questions
will yield insight into PAAT evolution and distribution across bacteria, identify strategies for targeted therapeutics,
and add to the fundamental knowledge of PAAT function and regulatory properties in bacteria.

## Key facts

- **NIH application ID:** 10134836
- **Project number:** 3R35GM133506-02S1
- **Recipient organization:** SAN FRANCISCO STATE UNIVERSITY
- **Principal Investigator:** Misty Kuhn
- **Activity code:** R35 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 2020
- **Award amount:** $171,005
- **Award type:** 3
- **Project period:** 2019-08-01 → 2024-05-31

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/10134836

## Citation

> US National Institutes of Health, RePORTER application 10134836, Investigating the structure, function, and regulation of polyamine acetyltransferases (3R35GM133506-02S1). Retrieved via AI Analytics 2026-05-23 from https://api.ai-analytics.org/grant/nih/10134836. Licensed CC0.

---

*[NIH grants dataset](/datasets/nih-grants) · CC0 1.0*