Regulation of pri-miRNA processing by the hnRNP-like protein AtGRP7 in Arabidopsis
Köster T, Meyer K, Weinholdt C, Smith LM, Lummer M, Speth C, Grosse I, Weigel D, Staiger D (2014)
Nucleic acids research 42(15): 9925-9936.
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Autor*in
Köster, TinoUniBi ;
Meyer, KatjaUniBi;
Weinholdt, Claus;
Smith, Lisa M.;
Lummer, MartinaUniBi;
Speth, Corinna;
Grosse, Ivo;
Weigel, Detlef;
Staiger, DorotheeUniBi
Abstract / Bemerkung
The hnRNP-like glycine-rich RNA-binding protein AtGRP7 regulates pre-mRNA splicing in Arabidopsis. Here we used small RNA-seq to show that AtGRP7 also affects the miRNA inventory. AtGRP7 overexpression caused a significant reduction in the level of 30 miRNAs and an increase for 14 miRNAs with a minimum log2 fold change of ±0.5. Overaccumulation of several pri-miRNAs including pri-miR398b, pri-miR398c, pri-miR172b, pri-miR159a and pri-miR390 at the expense of the mature miRNAs suggested that AtGRP7 affects pri-miRNA processing. Indeed, RNA immunoprecipitation revealed that AtGRP7 interacts with these pri-miRNAs in vivo. Mutation of an arginine in the RNA recognition motif abrogated in vivo binding and the effect on miRNA and pri-miRNA levels, indicating that AtGRP7 inhibits processing of these pri-miRNAs by direct binding. In contrast, pri-miRNAs of selected miRNAs that were elevated or not changed in response to high AtGRP7 levels were not bound in vivo. Reduced accumulation of miR390, an initiator of trans-acting small interfering RNA (ta-siRNA) formation, also led to lower TAS3 ta-siRNA levels and increased mRNA expression of the target AUXIN RESPONSE FACTOR4. Furthermore, AtGRP7 affected splicing of pri-miR172b and pri-miR162a. Thus, AtGRP7 is an hnRNP-like protein with a role in processing of pri-miRNAs in addition to its role in pre-mRNA splicing.
Erscheinungsjahr
2014
Zeitschriftentitel
Nucleic acids research
Band
42
Ausgabe
15
Seite(n)
9925-9936
ISSN
0305-1048
eISSN
1362-4962
Page URI
https://pub.uni-bielefeld.de/record/2694724
Zitieren
Köster T, Meyer K, Weinholdt C, et al. Regulation of pri-miRNA processing by the hnRNP-like protein AtGRP7 in Arabidopsis. Nucleic acids research. 2014;42(15):9925-9936.
Köster, T., Meyer, K., Weinholdt, C., Smith, L. M., Lummer, M., Speth, C., Grosse, I., et al. (2014). Regulation of pri-miRNA processing by the hnRNP-like protein AtGRP7 in Arabidopsis. Nucleic acids research, 42(15), 9925-9936. doi:10.1093/nar/gku716
Köster, Tino, Meyer, Katja, Weinholdt, Claus, Smith, Lisa M., Lummer, Martina, Speth, Corinna, Grosse, Ivo, Weigel, Detlef, and Staiger, Dorothee. 2014. “Regulation of pri-miRNA processing by the hnRNP-like protein AtGRP7 in Arabidopsis”. Nucleic acids research 42 (15): 9925-9936.
Köster, T., Meyer, K., Weinholdt, C., Smith, L. M., Lummer, M., Speth, C., Grosse, I., Weigel, D., and Staiger, D. (2014). Regulation of pri-miRNA processing by the hnRNP-like protein AtGRP7 in Arabidopsis. Nucleic acids research 42, 9925-9936.
Köster, T., et al., 2014. Regulation of pri-miRNA processing by the hnRNP-like protein AtGRP7 in Arabidopsis. Nucleic acids research, 42(15), p 9925-9936.
T. Köster, et al., “Regulation of pri-miRNA processing by the hnRNP-like protein AtGRP7 in Arabidopsis”, Nucleic acids research, vol. 42, 2014, pp. 9925-9936.
Köster, T., Meyer, K., Weinholdt, C., Smith, L.M., Lummer, M., Speth, C., Grosse, I., Weigel, D., Staiger, D.: Regulation of pri-miRNA processing by the hnRNP-like protein AtGRP7 in Arabidopsis. Nucleic acids research. 42, 9925-9936 (2014).
Köster, Tino, Meyer, Katja, Weinholdt, Claus, Smith, Lisa M., Lummer, Martina, Speth, Corinna, Grosse, Ivo, Weigel, Detlef, and Staiger, Dorothee. “Regulation of pri-miRNA processing by the hnRNP-like protein AtGRP7 in Arabidopsis”. Nucleic acids research 42.15 (2014): 9925-9936.
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Glycine-rich RNA-binding protein 7 (UNIPROT: F4IHK9)
Organism: Arabidopsis thaliana
Download in FASTA format
Organism: Arabidopsis thaliana
Download in FASTA format
Glycine-rich RNA-binding protein 7 (UNIPROT: Q03250)
Organism: Arabidopsis thaliana
Download in FASTA format
Organism: Arabidopsis thaliana
Download in FASTA format
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The SERRATE protein is involved in alternative splicing in Arabidopsis thaliana.
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