On the evolution of the tRNA-dependent amidotransferases, GatCAB and GatDE.

On the evolution of the tRNA-dependent amidotransferases, GatCAB and GatDE. Research Abstract Details 

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On the evolution of the tRNA-dependent amidotransferases, GatCAB and GatDE. Abstract Text:

Glutaminyl-tRNA synthetase and asparaginyl-tRNA synthetase evolved from glutamyl-tRNA synthetase and aspartyl-tRNA synthetase, respectively, after the split in the last universal communal ancestor (LUCA). Glutaminyl-tRNA(Gln) and asparaginyl-tRNA(Asn) were likely formed in LUCA by amidation of the mischarged species, glutamyl-tRNA(Gln) and aspartyl-tRNA(Asn), by tRNA-dependent amidotransferases, as is still the case in most bacteria and all known archaea. The amidotransferase GatCAB is found in both domains of life, while the heterodimeric amidotransferase GatDE is found only in Archaea. The GatB and GatE subunits belong to a unique protein family that includes Pet112 that is encoded in the nuclear genomes of numerous eukaryotes. GatE was thought to have evolved from GatB after the emergence of the modern lines of decent. Our phylogenetic analysis though places the split between GatE and GatB, prior to the phylogenetic divide between Bacteria and Archaea, and Pet112 to be of mitochondrial origin. In addition, GatD appears to have emerged prior to the bacterial-archaeal phylogenetic divide. Thus, while GatDE is an archaeal signature protein, it likely was present in LUCA together with GatCAB. Archaea retained both amidotransferases, while Bacteria emerged with only GatCAB. The presence of GatDE has favored a unique archaeal tRNA(Gln) that may be preventing the acquisition of glutaminyl-tRNA synthetase in Archaea. Archaeal GatCAB, on the other hand, has not favored a distinct tRNA(Asn), suggesting that tRNA(Asn) recognition is not a major barrier to the retention of asparaginyl-tRNA synthetase in many Archaea.

On the evolution of the tRNA-dependent amidotransferases, GatCAB and GatDE. Publishing Authors By Initials

For similar amino acids, peptides, and proteins: amino acids: rna, transfer, amino acyl research abstracts see: amino acids, peptides, and proteins: amino acids: rna, transfer, amino acyl research

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On the evolution of the tRNA-dependent amidotransferases, GatCAB and GatDE. Journal Published:

PUBLICATION TYPE: Research Support, U.S. Gov't,

Journal: Journal of molecular biology

VOLUME: 377

Page Numbers: 831-44

Journal Abbreviation: J. Mol. Biol.

ISSN: 1089-8638

DAY: 16

MONTH: 01

YEAR: 2008

On the evolution of the tRNA-dependent amidotransferases, GatCAB and GatDE. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 2985088

On the evolution of the tRNA-dependent amidotransferases, GatCAB and GatDE. Keywords Mesh Terms:

KEYWORDS: RNA, Transfer, Amino Acyl

MESH TERMS: genetics

Chemical & Substance for Abstract: On the evolution of the tRNA-dependent amidotransferases, GatCAB and GatDE. Information

Substance Name: asparaginyl-tRNA synthetase

Registry Number: EC 6.1.1.22

Grant and Affiliation Information for On the evolution of the tRNA-dependent amidotransferases, GatCAB and GatDE.

AFFILIATION: Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520-8114, USA.

Country: England

AGENCY: United States NIGMS

GRANT: GM22854

ACRONYM: GM

MEDLINETA: J Mol Biol

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