50 years ago protein synthesis met molecular biology: the discoveries of amino acid activation and transfer RNA

2005 ◽  
Vol 19 (12) ◽  
pp. 1583-1584 ◽  
Author(s):  
Thoru Pederson
Keyword(s):  
Protein Synthesis ◽  
Amino Acid ◽  
Molecular Biology ◽  
Transfer Rna ◽  
Acid Activation ◽  
Amino Acid Activation

Amino acid activation and protein synthesis

1959 ◽  
Vol 54 (S1) ◽  
pp. 75-88 ◽  
Author(s):  
Fritz Lipmann ◽  
W. C. H�lsmann ◽  
G. Hartmann ◽  
Hans G. Boman ◽  
George Acs
Keyword(s):  
Protein Synthesis ◽  
Amino Acid ◽  
Acid Activation ◽  
Amino Acid Activation

scholarly journals The mechanism of β-N-methylamino-l-alanine inhibition of tRNA aminoacylation and its impact on misincorporation

2019 ◽  
Vol 295 (5) ◽  
pp. 1402-1410 ◽  
Author(s):  
Nien-Ching Han ◽  
Tammy J. Bullwinkle ◽  
Kaeli F. Loeb ◽  
Kym F. Faull ◽  
Kyle Mohler ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Amino Acid ◽  
Direct Evidence ◽  
Trna Synthetase ◽  
Acid Activation ◽  
Aminoacyl Trna Synthetase ◽  
Amino Acid Activation ◽  
Biochemical Assays ◽  
Serine Codons ◽  
Lateral Sclerosis

β-N-methylamino-l-alanine (BMAA) is a nonproteinogenic amino acid that has been associated with neurodegenerative diseases, including amyotrophic lateral sclerosis (ALS) and Alzheimer's disease (AD). BMAA has been found in human protein extracts; however, the mechanism by which it enters the proteome is still unclear. It has been suggested that BMAA is misincorporated at serine codons during protein synthesis, but direct evidence of its cotranslational incorporation is currently lacking. Here, using LC-MS–purified BMAA and several biochemical assays, we sought to determine whether any aminoacyl-tRNA synthetase (aaRS) utilizes BMAA as a substrate for aminoacylation. Despite BMAA's previously predicted misincorporation at serine codons, following a screen for amino acid activation in ATP/PPi exchange assays, we observed that BMAA is not a substrate for human seryl-tRNA synthetase (SerRS). Instead, we observed that BMAA is a substrate for human alanyl-tRNA synthetase (AlaRS) and can form BMAA-tRNAAla by escaping from the intrinsic AlaRS proofreading activity. Furthermore, we found that BMAA inhibits both the cognate amino acid activation and the editing functions of AlaRS. Our results reveal that, in addition to being misincorporated during translation, BMAA may be able to disrupt the integrity of protein synthesis through multiple different mechanisms.

Amino acid activation for protein synthesis in Plasmodium berghei

1969 ◽  
Vol 134 (9) ◽  
pp. 1026-1031 ◽  
Author(s):  
J. Ilan ◽  
Judith Ilan ◽  
K. Tokuyasu
Keyword(s):  
Protein Synthesis ◽  
Amino Acid ◽  
Plasmodium Berghei ◽  
Acid Activation ◽  
Amino Acid Activation

scholarly journals Streptogramin B biosynthesis in Streptomyces pristinaespiralis and Streptomyces virginiae: molecular characterization of the last structural peptide synthetase gene.

1997 ◽  
Vol 41 (9) ◽  
pp. 1904-1909 ◽  
Author(s):  
V de Crécy-Lagard ◽  
W Saurin ◽  
D Thibaut ◽  
P Gil ◽  
L Naudin ◽  
...  
Keyword(s):  
Amino Acid ◽  
Acid Activation ◽  
Activation Domains ◽  
Amino Acid Activation ◽  
Streptomyces Virginiae ◽  
Streptomyces Pristinaespiralis ◽  
Degenerate Oligonucleotide ◽  
Peptide Synthetase ◽  
Different Origins

Streptomyces pristinaespiralis and S. virginiae both produce closely related hexadepsipeptide antibiotics of the streptogramin B family. Pristinamycins I and virginiamycins S differ only in the fifth incorporated precursor, di(mono)methylated amine and phenylalanine, respectively. By using degenerate oligonucleotide probes derived from internal sequences of the purified S. pristinaespiralis SnbD and SnbE proteins, the genes from two streptogramin B producers, S. pristinaespiralis and S. virginiae, encoding the peptide synthetase involved in the activation and incorporation of the last four precursors (proline, 4-dimethylparaaminophenylalanine [for pristinamycin I(A)] or phenylalanine [for virginiamycin S], pipecolic acid, and phenylglycine) were cloned. Analysis of the sequence revealed that SnbD and SnbE are encoded by a unique snbDE gene. SnbDE (4,849 amino acids [aa]) contains four amino acid activation domains, four condensation domains, an N-methylation domain, and a C-terminal thioesterase domain. Comparison of the sequences of 55 amino acid-activating modules from different origins confirmed that these sequences contain enough information for the performance of legitimate predictions of their substrate specificity. Partial sequencing (1,993 aa) of the SnbDE protein of S. virginiae allowed comparison of the proline and aromatic acid activation domains of the two species and the identification of coupled frameshift mutations.

scholarly journals The Mechanism of Amino Acid Activation: the Work of Mahlon Hoagland

2009 ◽  
Vol 284 (25) ◽  
pp. e7-e8
Author(s):  
Nicole Kresge ◽  
Robert D. Simoni ◽  
Robert L. Hill
Keyword(s):  
Amino Acid ◽  
Acid Activation ◽  
Amino Acid Activation
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