N-degron specificity of chloroplast ClpS1 in plants

FEBS Letters

article

Cyrille Montandon¹  David A. Dougan²  Klaas J. van Wijk¹ 

[1] Plant Biology Section, School of Integrative Plant Sciences (SIPS), Cornell University;Department of Biochemistry and Genetics, La Trobe Institute for Molecular Science, La Trobe University

关键词: adaptor;    Arabidopsis thaliana;    chloroplast;    ClpS1;    N-degron;    protease;   

DOI  :  10.1002/1873-3468.13378

来源: John Wiley & Sons Ltd.

【 摘 要 】

tRNAHis guanylyltransferase (Thg1) specifies eukaryotic tRNAHis identity by catalysing a 30 –50 non-Watson–Crick (WC) addition of guanosine to the 50 -end of tRNAHis. Thg1 family enzymes in Archaea and Bacteria, called Thg1-like proteins (TLPs), catalyse a similar but distinct 30 –50 addition in an exclusively WC-dependent manner. Here, a genetic system in Saccharomyces cerevisiae was employed to further assess the biochemical differences between Thg1 and TLPs. Utilizing a novel 50 -end sequencing pipeline, we find that a Bacillus thuringiensis TLP sustains the growth of a thg1D strain by maintaining a WC-dependent addition of U1 across from A73. Additionally, we observe 50 -end heterogeneity in S. cerevisiae small nucleolar RNAs (snoRNAs), an observation that may inform methods of annotation and mechanisms of snoRNA processing.

【 授权许可】

Unknown