PMID: 9177188Jun 10, 1997Paper

Expression of a gene encoding a tRNA synthetase-like protein is enhanced in tumorigenic human myeloid leukemia cells and is cell cycle stage- and differentiation-dependent

Proceedings of the National Academy of Sciences of the United States of America
S SenR A White

Abstract

We cloned a tumorigenic phenotype-associated cDNA encoding a tRNA synthetase-like protein from an acute-phase human myeloid leukemia cell line. The cDNA was isolated by reiterative subtraction of cDNAs synthesized from tumor-generating parental leukemia cells versus those from a nontumorigenic variant of the same cells. The selected cDNA encodes a protein that is a close homolog of one subunit of prokaryote and yeast phenylalanyl-tRNA synthetase (PheRS). The expressed protein reacts specificially with polyclonal antibodies raised against mammalian phenylalanyl-tRNA synthetase. Expression of the gene (designated CML33) was directly confirmed by Northern blot hybridization to be substantially enhanced in the tumorigenic cells compared with the nontumorigenic variant. In addition, expression of CML33 in myeloid leukemia cells was sensitive to the stage of the cell cycle and to induction of differentiation. Although the relationship between these observations and the tumorigenic state of the human myeloid leukemia cell line used in these studies is unknown, to our knowledge, this is the first demonstration in mammalian cells of tumor-selective and cell cycle stage- and differentiation-dependent expression of a member of the tRNA sy...Continue Reading

References

Dec 1, 1977·Proceedings of the National Academy of Sciences of the United States of America·F SangerA R Coulson
Jun 1, 1979·Proceedings of the National Academy of Sciences of the United States of America·G RoveraC Damsky
Apr 1, 1992·Trends in Biochemical Sciences·D Moras
Dec 15, 1991·Proceedings of the National Academy of Sciences of the United States of America·E C Uberbacher, R J Mural
Oct 1, 1991·Proceedings of the National Academy of Sciences of the United States of America·A SanniF Fasiolo
May 1, 1990·Genetic Analysis, Techniques and Applications·C W SchweinfestT S Papas
Apr 6, 1988·Journal of the National Cancer Institute·P S SteegM E Sobel
Dec 15, 1983·Journal of Molecular Biology·M SpringerM Grunberg-Manago
Jul 1, 1995·Nature Structural Biology·L MosyakM G Safro
Nov 1, 1995·Protein Science : a Publication of the Protein Society·M Safro, L Mosyak

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Citations

Dec 9, 2003·Journal of Biosciences·Jyoti K Jaiswal, Vidyanand Nanjundiah
Feb 6, 2009·Acta Crystallographica. Section F, Structural Biology and Crystallization Communications·Igal FinarovMark Safro
Feb 8, 2006·FEBS Letters·Flavia Cristina Rodrigues-LisoniEgle Solito
Apr 1, 2015·Database : the Journal of Biological Databases and Curation·Ji-Hyun LeeSunghoon Kim
Jun 30, 2012·PloS One·Verónica Martínez-CerdeñoPaul S Knoepfler
May 18, 1999·Journal of Molecular Biology·J M BullardL L Spremulli
Jun 20, 1998·Journal of Molecular Biology·A Lechler, R Kreutzer
Feb 7, 2021·Disease Models & Mechanisms·Manh Tin HoBeat Suter

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