Resonance assignments of La protein RRM domain from Trypanosoma brucei
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ARTICLE
Resonance assignments of La protein RRM domain from Trypanosoma brucei Fangzhen Shan1,2 · Nannan Zhang3 Received: 28 June 2020 / Accepted: 20 October 2020 © Springer Nature B.V. 2020
Abstract The autoantigen La protein is a conserved component of eukaryotic ribonucleoprotein complexes that binds the 3′ poly(U) sequences of nascent RNA polymerase III transcripts to assist folding and maturation. This specific recognition is mediated by the N-terminal domain (NTD) of La, which comprises a La motif and an RNA recognition motif (RRM). Here, we report near complete 1H, 13C and 15N backbone and sidechain assignments for the RRM domain of La protein from Trypanosoma brucei. Keywords RRM domain · La protein · T. brucei · Resonance assignment
Biological context The La protein is a phosphoprotein expressed in a variety of different organisms, including trypanosome, yeast, and plant (Maraia and Intine 2002; Wolin and Cedervall 2002). Originally identified as an autoantigen associated with rheumatic diseases such as lupus erythematosus and Sjogren’s syndrome, La has been shown to have key roles in the processing and use of coding and noncoding RNAs (Alspaugh and Tan 1975; Mattioli and Reichlin 1974). Experiments in which patient anti-La antibodies were used to immunoprecipitate La ribonucleoproteins (RNPs) from radiolabeled cell extracts revealed that the La protein associated with a very large number of nascent small RNAs, including pretRNAs, pre-5S rRNA, U6 small nuclear RNA (snRNA), RNase P RNA, MRP RNA, 7SL RNA, Y RNAs (Hendrick et al. 1981; Lerner et al. 1981; Rinke and Steitz 1982; Wolin and Cedervall 2002). For the majority of cellular RNAs, La protein binds the precursors, rather than the mature * Nannan Zhang [email protected] 1
Medical Research Center, Affiliated Hospital of Jining Medical University, Jining 272029, Shandong, China
2
Hefei National Laboratory for Physical Science At Microscale and School of Life Science, University of Science and Technology of China, Hefei 230026, Anhui, China
3
Department of Pulmonary and Critical Care Medicine, Affiliated Hospital of Jining Medical University, Jining 272029, Shandong, China
RNAs. The La protein recognizes all of these nascent RNAs because it binds the sequence UUU-OH, which is the 3′ end of most newly synthesized polymerase III transcripts (Stefano 1984). Recognition of UUU-OH sequences is a function of the N-terminal domain (NTD), the most conserved portion of the protein, containing two subdomains, the La motif and the RRM domain. In this process, those two motifs co-operatively participate in binding pre-tRNA, and neither is dispensable (Alfano et al. 2004; Dong et al. 2004). The RRM domain in such abundance is necessarily biologically important and associated with many functions in the cell (Clery et al. 2008; Muto and Yokoyama 2012; Shan et al. 2019b). Indeed, RRM-containing proteins are involved in all post-transcriptional events: pre-mRNA processing, alternative splicing, mRNA stability, RNA editing, mRNA export, pre-rRNA com
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