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© The Rockefeller University Press, 0021-9525/2000//567 $5.00
The Journal of Cell Biology, Volume 149, Number 3, , 2000 567-574

Original Article

Nucleolar Localization of Human Methionyl–Trna Synthetase and Its Role in Ribosomal RNA Synthesis



Young-Gyu Koa, Young-Sun Kanga, Eun-Kyoung Kima, Sang Gyu Parka, and Sunghoon Kima

a National Creative Research Initiatives Center for ARS Network, Sung Kyun Kwan University, Jangangu, Suwon, Kyunggido 440-746, Korea
National Creative Research Initiatives Center for ARS Network, Sung Kyun Kwan University, 300 Chunchundong, Jangangu, Suwon, Kyunggido 440-746, Korea.82-331-290-568282-331-290-5681

shkim{at}yurim.skku.ac.kr

Human aminoacyl–tRNA synthetases (ARSs) are normally located in cytoplasm and are involved in protein synthesis. In the present work, we found that human methionyl–tRNA synthetase (MRS) was translocated to nucleolus in proliferative cells, but disappeared in quiescent cells. The nucleolar localization of MRS was triggered by various growth factors such as insulin, PDGF, and EGF. The presence of MRS in nucleoli depended on the integrity of RNA and the activity of RNA polymerase I in the nucleolus. The ribosomal RNA synthesis was specifically decreased by the treatment of anti-MRS antibody as determined by nuclear run-on assay and immunostaining with anti-Br antibody after incorporating Br-UTP into nascent RNA. Thus, human MRS plays a role in the biogenesis of rRNA in nucleoli, while it is catalytically involved in protein synthesis in cytoplasm.

Key Words: methionyl–tRNA synthetase • nucleoli • growth signal • ribosomal RNA synthesis • RNA polymerase I

© 2000 The Rockefeller University Press

Young-Gyu Ko and Young-Sun Kang contributed equally to this work.

Abbreviations used in this paper: ARSs, aminoacyl–tRNA synthetases; EPRS, bifunctional glutamyl-prolyl–tRNA synthetase; Hsp90, heat shock protein 90; MRS, methionyl–tRNA synthetase; QRS, glutaminyl–tRNA synthetase; RRS, arginyl–tRNA synthetase.


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