# 1H, 13C and 15N resonance assignments for the acetyltransferase domain of the kinetoplastid kinetochore protein KKT23 from Trypanosoma brucei

## TL;DR

This paper reports resonance assignments for a histone acetyltransferase domain of the KKT23 protein from Trypanosoma brucei, aiding in understanding its structure and function.

## Contribution

The study provides new NMR resonance assignments for the KKT23 acetyltransferase domain in complex with cofactors.

## Key findings

- Resonance assignments for KKT23125–348 in complex with acetyl coenzyme A and coenzyme A are reported.
- The data will support further structural and dynamic studies of KKT23 in solution.

## Abstract

KKT23 is a kinetoplastid-specific kinetochore protein that has a C-terminal GCN5-related histone acetyltransferase domain that acetylates the C-terminal tail of histone H2A. Here, we present the 1H, 13C and 15N resonance assignments for the C-terminal region of KKT23 (KKT23125–348) from Trypanosoma brucei in complex with known cofactors for acetyltransferases, acetyl coenzyme A and coenzyme A. These assignments provide the starting point for detailed investigation of the structure, dynamics and interactions of KKT23 in solution.

The online version contains supplementary material available at 10.1007/s12104-025-10235-4.