Nucleolar targeting in an early-branching eukaryote suggests a general mechanism for ribosome protein sorting.

ABSTRACT: The compartmentalised eukaryotic cell demands accurate targeting of proteins to the organelles in which they function, whether membrane-bound (like the nucleus) or non-membrane-bound (like the nucleolus). Nucleolar targeting relies on positively charged localisation signals and has received rejuvenated interest since the widespread recognition of liquid-liquid phase separation (LLPS) as a mechanism contributing to nucleolus formation. Here, we exploit a new genome-wide analysis of protein localisation in the early-branching eukaryote Trypanosoma brucei to analyse general nucleolar protein properties. T. brucei nucleolar proteins have similar properties to those in common model eukaryotes, specifically basic amino acids. Using protein truncations and addition of candidate targeting sequence

SUBMITTER: Jeilani M 

PROVIDER: S-EPMC9659390 | biostudies-literature | 2022 Oct

REPOSITORIES: biostudies-literature