Literature summary for 6.1.1.5 extracted from

Kermgard, E.; Yang, Z.; Michel, A.M.; Simari, R.; Wong, J.; Ibba, M.; Lazazzera, B.A.
Quality control by isoleucyl-tRNA synthetase of Bacillus subtilis is required for efficient sporulation (2017), Sci. Rep., 7, 41763 .

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Cloned(Commentary)

Cloned (Comment)	Organism
subcloning and expression of wild-type and mutant enzymes in Escherichia coli Top10 cells	Bacillus subtilis

Protein Variants

Protein Variants	Comment	Organism
T233P	site-directed mutagenesis, mutant ileS(T233P) allows tRNAIle mischarging while retaining wild-type Ile-tRNAIle synthesis activity. The growth rate of the ileS(T233P)strain is not significantly different from wild-type. The ileS(T233P) strain is observed to exhibit a significant defect in formation of environmentally resistant spores. The sporulation defect ranges from 3fold to 30fold and is due to a delay in activation of early sporulation genes. The loss of aminoacylation quality control in the ileS(T233P) strain results in the inability to compete with a wild-type strain under selective conditions that require sporulation	Bacillus subtilis

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	required	Bacillus subtilis

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
ATP + L-isoleucine + tRNAIle	Bacillus subtilis	-	AMP + diphosphate + L-isoleucyl-tRNAIle	-	?
ATP + L-isoleucine + tRNAIle	Bacillus subtilis BAL4574	-	AMP + diphosphate + L-isoleucyl-tRNAIle	-	?

Organism

Organism	UniProt	Comment	Textmining
Bacillus subtilis	-	a derivative of the JH642 strain	-
Bacillus subtilis BAL4574	-	a derivative of the JH642 strain	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + L-isoleucine + tRNAIle	-	Bacillus subtilis	AMP + diphosphate + L-isoleucyl-tRNAIle	-	?
ATP + L-isoleucine + tRNAIle	-	Bacillus subtilis BAL4574	AMP + diphosphate + L-isoleucyl-tRNAIle	-	?

Synonyms

Synonyms	Comment	Organism
IleRS	-	Bacillus subtilis
Isoleucyl-tRNA synthetase	-	Bacillus subtilis

Cofactor

Cofactor	Comment	Organism	Structure
ATP	-	Bacillus subtilis

General Information

General Information	Comment	Organism
malfunction	mutant ileS(T233P) allows tRNAIle mischarging while retaining wild-type Ile-tRNAIle synthesis activity. The growth rate of the ileS(T233P) strain BAL4571 is not significantly different from wild-type strain BAL4574. The ileS(T233P) strain is observed to exhibit a significant defect in formation of environmentally resistant spores. The sporulation defect ranges from 3fold to 30fold and is due to a delay in activation of early sporulation genes. The loss of aminoacylation quality control in the ileS(T233P) strain results in the inability to compete with a wild-type strain under selective conditions that require sporulation. The quality control-defective IleRS mutant is defective in expressing genes activated by the master regulator of sporulation, Spo0A. Phenotype, overview. Spo0A is the first transcription factor to become active, through phosphorylation by a phosphorelay, in the sporulation regulatory cascade	Bacillus subtilis
physiological function	isoleucyl-tRNA synthetase (IleRS) is an aminoacyl-tRNA synthetase whose essential function is to aminoacylate tRNAIle with isoleucine. Like some other aminoacyl-tRNA synthetases, IleRS can mischarge tRNAIle and correct this misacylation through a separate post-transfer editing function, biological significance of this editing function. The quality control function of IleRS is required in Bacillus subtilis for efficient sporulation and editing by aminoacyl-tRNA synthetases may be important for survival under starvation/nutrient limitation conditions. Isoleucine-tRNA synthetase (IleRS) possesses quality control functions that discriminate between isoleucine, the non-cognate amino acid valine, and the non-proteinogenic amino acids, norvaline, a by-product of branched-chain amino acid synthesis, and homocysteine (Hcy), a by-product from degradation of S-adenosylhomocysteine by LuxS in bacteria	Bacillus subtilis

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Release 2023.1 (January 2023)