Discovery of human cytosolic leucyl-tRNA synthetase CP hairpin domain function

On July 29th, the international academic journal RNA published the latest research results of the Wang Enduo research group of the Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, and analyzed the human cytoplasmic leucyl-tRNA synthetase. The function and mechanism of the CP hairpin domain in the enzymatic process.


Leucyl-tRNA synthetase (LeuRS) catalyzes the esterification reaction between leucine and the corresponding tRNALeu. The structures of leucine and isoleucine, methionine and norvaline are very similar, and the leucine-tRNA synthetase has a low ability to discriminate the above amino acids, and it is possible to generate the wrong aminoacyl-tRNALeu. In evolution, leucyl-tRNA synthetase recruited new editing domains on top of the original catalytic domain to hydrolyze the amino-acylation products to ensure that the protein translation process proceeds correctly. The amino acid sequence between the linking catalytic domain and the editing domain is referred to as the CP hairpin domain. It is generally believed that this domain may maintain the spatial structure of the enzyme and participate in the conformational changes in the enzymatic process, but little is known about its details.


Huang Yu, a researcher from the Wang Enduo research group, deleted the CP hairpin domain of human cytosolic leucyl-tRNA synthetase and found that the amino acid activation ability and aminoacylation ability of the enzyme were completely lost, and the tRNA binding ability was greatly weakened. And the editing function is almost unaffected. They constructed a series of chimeric leucyl-tRNA synthetases of prokaryotic, eukaryotic and archaea, and found that only the leucyl-tRNA synthetase CP hairpin domain from eukaryotic yeast can replace human cytoplasmic bright ammonia. The function of the acyl-tRNA synthetase CP hairpin domain. Through structural and sequence analysis, it was found that the flexible amino acid residues of this domain are involved in the conformational change in the enzymatic process, which is essential for the amino acid activation ability and aminoacylation ability of the enzyme, while the polar amino acid residues are Responsible for the binding process of the enzyme to tRNALeu.


This result helps people better understand the catalytic principle of leucyl-tRNA synthetase and finds structural differences between human cytosolic leucyl-tRNA synthetase and pathogenic bacteria leucyl-tRNA synthetase. Sexually design new antibiotic drugs.


Various products of Toilet Roll, providing product images and basic parameters with each Toilet Tissue Roll and Toilet Tissue Paper; We are a professional Chinese manufacturer of Toilet Roll, and look forward to your cooperation!

Dissolvable toilet roll hygiene toilet tissue Toilet roll paper /bathroom tissues Comfortable softness and more comfortable to use.

Don't worry about clogging the toilet .This Toilet Roll has strong water absorbent. Easily dissolved in water, and then no dust free of power and no harmful chemicals. Factory directly supply/ competitive price/reliable quality/unworried sales service


Toilet Roll

Toilet Tissue Roll,Toilet Tissue Paper,Softest Toilet Paper,Tubeless Toilet Paper

Yafeng Paper Industry Co., Ltd , https://www.tenoutissue.com

Posted on