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Aminoacylation of hypomodified tRNAGlu in vivo

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Aminoacylation of hypomodified tRNAGlu in vivo. / Krüger, Malene Kappen; Sørensen, M.A.

I: Journal of Molecular Biology, Bind 284, Nr. 3, 1998, s. 609-620.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Harvard

Krüger, MK & Sørensen, MA 1998, 'Aminoacylation of hypomodified tRNAGlu in vivo', Journal of Molecular Biology, bind 284, nr. 3, s. 609-620. https://doi.org/10.1006/jmbi.1998.2197

APA

Krüger, M. K., & Sørensen, M. A. (1998). Aminoacylation of hypomodified tRNAGlu in vivo. Journal of Molecular Biology, 284(3), 609-620. https://doi.org/10.1006/jmbi.1998.2197

Vancouver

Krüger MK, Sørensen MA. Aminoacylation of hypomodified tRNAGlu in vivo. Journal of Molecular Biology. 1998;284(3):609-620. https://doi.org/10.1006/jmbi.1998.2197

Author

Krüger, Malene Kappen ; Sørensen, M.A. / Aminoacylation of hypomodified tRNAGlu in vivo. I: Journal of Molecular Biology. 1998 ; Bind 284, Nr. 3. s. 609-620.

Bibtex

@article{c8fe022074c911dbbee902004c4f4f50,
title = "Aminoacylation of hypomodified tRNAGlu in vivo",
abstract = "The highly specific interaction of each aminoacyl-tRNA synthetase and its substrate tRNAs constitutes an intriguing problem in protein-RNA recognition. All tRNAs have the same overall three-dimensional structure in order to fit interchangeably into the translational apparatus. Thus, the recognition by aminoacyl-tRNA synthetase must be more or less limited to discrimination between bases at specific positions within the tRNA. The hypermodified nucleotide 5-methylaminomethyl-2-thiouridine (mnm5s2U) present at the wobble position of bacterial tRNAs specific for glutamic acid, lysine and possibly glutamine has been shown to be important in the recognition of these tRNAs by their synthetases in vitro. Here, we have determined the aminoacylation level in vivo of tRNAGlu, tRNALys, and tRNA1GIn in Escherichia coli strains containing undermodified derivatives of mnm5s2U34. Lack of the 5-methylaminomethyl group did not reduce charging levels for any of the three tRNAs. Lack of the s2U34 modification caused a 40% reduction in the charging level of tRNAGlu. Charging of tRNALysand tRNA1Gln were less affected. There was no compensating regulation of expression of glutamyl-tRNA synthetase because the relative synthesis rate was the same in the wild-type and mutant strains. These results indicate that the mnm5U34 modification is not an important recognition element in vivo for the glutamyl-tRNA synthetase. In contrast, lack of the s2U34 modification reduced the efficiency of charging by at least 40%. This is the minimal estimate because the turn-over rate of Glu-tRNAGlu was also reduced in the absence of the 2-thio group. Lack of either modification did not affect mischarging or mistranslation.",
author = "Kr{\"u}ger, {Malene Kappen} and M.A. S{\o}rensen",
note = "Keywords: in vivo aminoacylation level; glutamyl-tRNA synthetase; tRNA identity; AsuE; TrmE",
year = "1998",
doi = "10.1006/jmbi.1998.2197",
language = "English",
volume = "284",
pages = "609--620",
journal = "Journal of Molecular Biology",
issn = "0022-2836",
publisher = "Academic Press",
number = "3",

}

RIS

TY - JOUR

T1 - Aminoacylation of hypomodified tRNAGlu in vivo

AU - Krüger, Malene Kappen

AU - Sørensen, M.A.

N1 - Keywords: in vivo aminoacylation level; glutamyl-tRNA synthetase; tRNA identity; AsuE; TrmE

PY - 1998

Y1 - 1998

N2 - The highly specific interaction of each aminoacyl-tRNA synthetase and its substrate tRNAs constitutes an intriguing problem in protein-RNA recognition. All tRNAs have the same overall three-dimensional structure in order to fit interchangeably into the translational apparatus. Thus, the recognition by aminoacyl-tRNA synthetase must be more or less limited to discrimination between bases at specific positions within the tRNA. The hypermodified nucleotide 5-methylaminomethyl-2-thiouridine (mnm5s2U) present at the wobble position of bacterial tRNAs specific for glutamic acid, lysine and possibly glutamine has been shown to be important in the recognition of these tRNAs by their synthetases in vitro. Here, we have determined the aminoacylation level in vivo of tRNAGlu, tRNALys, and tRNA1GIn in Escherichia coli strains containing undermodified derivatives of mnm5s2U34. Lack of the 5-methylaminomethyl group did not reduce charging levels for any of the three tRNAs. Lack of the s2U34 modification caused a 40% reduction in the charging level of tRNAGlu. Charging of tRNALysand tRNA1Gln were less affected. There was no compensating regulation of expression of glutamyl-tRNA synthetase because the relative synthesis rate was the same in the wild-type and mutant strains. These results indicate that the mnm5U34 modification is not an important recognition element in vivo for the glutamyl-tRNA synthetase. In contrast, lack of the s2U34 modification reduced the efficiency of charging by at least 40%. This is the minimal estimate because the turn-over rate of Glu-tRNAGlu was also reduced in the absence of the 2-thio group. Lack of either modification did not affect mischarging or mistranslation.

AB - The highly specific interaction of each aminoacyl-tRNA synthetase and its substrate tRNAs constitutes an intriguing problem in protein-RNA recognition. All tRNAs have the same overall three-dimensional structure in order to fit interchangeably into the translational apparatus. Thus, the recognition by aminoacyl-tRNA synthetase must be more or less limited to discrimination between bases at specific positions within the tRNA. The hypermodified nucleotide 5-methylaminomethyl-2-thiouridine (mnm5s2U) present at the wobble position of bacterial tRNAs specific for glutamic acid, lysine and possibly glutamine has been shown to be important in the recognition of these tRNAs by their synthetases in vitro. Here, we have determined the aminoacylation level in vivo of tRNAGlu, tRNALys, and tRNA1GIn in Escherichia coli strains containing undermodified derivatives of mnm5s2U34. Lack of the 5-methylaminomethyl group did not reduce charging levels for any of the three tRNAs. Lack of the s2U34 modification caused a 40% reduction in the charging level of tRNAGlu. Charging of tRNALysand tRNA1Gln were less affected. There was no compensating regulation of expression of glutamyl-tRNA synthetase because the relative synthesis rate was the same in the wild-type and mutant strains. These results indicate that the mnm5U34 modification is not an important recognition element in vivo for the glutamyl-tRNA synthetase. In contrast, lack of the s2U34 modification reduced the efficiency of charging by at least 40%. This is the minimal estimate because the turn-over rate of Glu-tRNAGlu was also reduced in the absence of the 2-thio group. Lack of either modification did not affect mischarging or mistranslation.

U2 - 10.1006/jmbi.1998.2197

DO - 10.1006/jmbi.1998.2197

M3 - Journal article

C2 - 9826502

VL - 284

SP - 609

EP - 620

JO - Journal of Molecular Biology

JF - Journal of Molecular Biology

SN - 0022-2836

IS - 3

ER -

ID: 205394