ß-Lysine discrimination by lysyl-tRNA synthetase

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Standard

ß-Lysine discrimination by lysyl-tRNA synthetase. / Gilreath, Marla S; Roy, Hervé; Bullwinkle, Tammy J; Katz, Assaf; Navarre, William W; Ibba, Michael.

I: F E B S Letters, Bind 585, Nr. 20, 2011, s. 3284-8.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Gilreath, MS, Roy, H, Bullwinkle, TJ, Katz, A, Navarre, WW & Ibba, M 2011, 'ß-Lysine discrimination by lysyl-tRNA synthetase', F E B S Letters, bind 585, nr. 20, s. 3284-8. https://doi.org/10.1016/j.febslet.2011.09.008

APA

Gilreath, M. S., Roy, H., Bullwinkle, T. J., Katz, A., Navarre, W. W., & Ibba, M. (2011). ß-Lysine discrimination by lysyl-tRNA synthetase. F E B S Letters, 585(20), 3284-8. https://doi.org/10.1016/j.febslet.2011.09.008

Vancouver

Gilreath MS, Roy H, Bullwinkle TJ, Katz A, Navarre WW, Ibba M. ß-Lysine discrimination by lysyl-tRNA synthetase. F E B S Letters. 2011;585(20):3284-8. https://doi.org/10.1016/j.febslet.2011.09.008

Author

Gilreath, Marla S ; Roy, Hervé ; Bullwinkle, Tammy J ; Katz, Assaf ; Navarre, William W ; Ibba, Michael. / ß-Lysine discrimination by lysyl-tRNA synthetase. I: F E B S Letters. 2011 ; Bind 585, Nr. 20. s. 3284-8.

Bibtex

@article{434b8f7cfd094d47839da2c61390fbef,

title = "{\ss}-Lysine discrimination by lysyl-tRNA synthetase",

abstract = "Elongation factor P is modified with (R)-{\ss}-lysine by the lysyl-tRNA synthetase (LysRS) paralog PoxA. PoxA specificity is orthogonal to LysRS, despite their high similarity. To investigate a- and {\ss}-lysine recognition by LysRS and PoxA, amino acid replacements were made in the LysRS active site guided by the PoxA structure. A233S LysRS behaved as wild type with a-lysine, while the G469A and A233S/G469A variants decreased stable a-lysyl-adenylate formation. A233S LysRS recognized {\ss}-lysine better than wildtype, suggesting a role for this residue in discriminating a- and {\ss}-amino acids. Both enantiomers of {\ss}-lysine were substrates for tRNA aminoacylation by LysRS, which, together with the relaxed specificity of the A233S variant, suggest a possible means to develop systems for in vivo co-translational insertion of {\ss}-amino acids.",

keywords = "Amino Acid Substitution, Bacillus cereus, Bacterial Proteins, Lysine, Lysine-tRNA Ligase, Mutation, Missense, Peptide Elongation Factors",

author = "Gilreath, {Marla S} and Herv{\'e} Roy and Bullwinkle, {Tammy J} and Assaf Katz and Navarre, {William W} and Michael Ibba",

year = "2011",

doi = "10.1016/j.febslet.2011.09.008",

language = "English",

volume = "585",

pages = "3284--8",

journal = "F E B S Letters",

issn = "0014-5793",

publisher = "JohnWiley & Sons Ltd",

number = "20",

}

RIS

TY - JOUR

T1 - ß-Lysine discrimination by lysyl-tRNA synthetase

AU - Gilreath, Marla S

AU - Roy, Hervé

AU - Bullwinkle, Tammy J

AU - Katz, Assaf

AU - Navarre, William W

AU - Ibba, Michael

PY - 2011

Y1 - 2011

N2 - Elongation factor P is modified with (R)-ß-lysine by the lysyl-tRNA synthetase (LysRS) paralog PoxA. PoxA specificity is orthogonal to LysRS, despite their high similarity. To investigate a- and ß-lysine recognition by LysRS and PoxA, amino acid replacements were made in the LysRS active site guided by the PoxA structure. A233S LysRS behaved as wild type with a-lysine, while the G469A and A233S/G469A variants decreased stable a-lysyl-adenylate formation. A233S LysRS recognized ß-lysine better than wildtype, suggesting a role for this residue in discriminating a- and ß-amino acids. Both enantiomers of ß-lysine were substrates for tRNA aminoacylation by LysRS, which, together with the relaxed specificity of the A233S variant, suggest a possible means to develop systems for in vivo co-translational insertion of ß-amino acids.

AB - Elongation factor P is modified with (R)-ß-lysine by the lysyl-tRNA synthetase (LysRS) paralog PoxA. PoxA specificity is orthogonal to LysRS, despite their high similarity. To investigate a- and ß-lysine recognition by LysRS and PoxA, amino acid replacements were made in the LysRS active site guided by the PoxA structure. A233S LysRS behaved as wild type with a-lysine, while the G469A and A233S/G469A variants decreased stable a-lysyl-adenylate formation. A233S LysRS recognized ß-lysine better than wildtype, suggesting a role for this residue in discriminating a- and ß-amino acids. Both enantiomers of ß-lysine were substrates for tRNA aminoacylation by LysRS, which, together with the relaxed specificity of the A233S variant, suggest a possible means to develop systems for in vivo co-translational insertion of ß-amino acids.

KW - Amino Acid Substitution

KW - Bacillus cereus

KW - Bacterial Proteins

KW - Lysine

KW - Lysine-tRNA Ligase

KW - Mutation, Missense

KW - Peptide Elongation Factors

U2 - 10.1016/j.febslet.2011.09.008

DO - 10.1016/j.febslet.2011.09.008

M3 - Journal article

C2 - 21925499

VL - 585

SP - 3284

EP - 3288

JO - F E B S Letters

JF - F E B S Letters

SN - 0014-5793

IS - 20

ER -

ID: 38488882