Progeline is a non-corresponding amino acid that has the greatest stress on the brewing yeast luminescide-tRNA synthase.

On June 3rd, Nucleic Acids Research, an international academic journal, published online the latest research by Wang Endo of the Institute of Biochemistry and Cell Biology of the Shanghai Institute of Life Sciences of the Chinese Academy of Sciences.
the editing function of the aminoacyl-tRNA synthase (aaRS) is responsible for hydrolyzing amino acids that are mis-activeed or misamino-ammylated, and for quality control of protein synthesis.
once the editing function of a particular aARS is impaired, it can lead to non-corresponding amino acids mistakenly mixed with proteins, causing proteins to fold by mistake and synthesize out of control.
to cope with the pressure caused by aaRS editing functional defects, cells have evolved a series of protective coping mechanisms.
Under the guidance of researcher Wang Endo, Ph.D. students Ji Quanquan and Fang Zhipeng, among others, demonstrated that positive proline (norvaline, Nva) is the most coercive non-amino acid against the brewing yeast leucyl-tRNA synthase (Saccharomyces cerevisiae leucyl-tRNA synthase, ScLeuRS).
Nva can be mistakenly mixed into the proteomics of LeuRS-edited functionally defective yeast cells (D419A/Sc?leuS), resulting in slower cell growth and even death.
cells up to Hsp70 to help misfold proteins to fold again.
A.Leu's similarity Nva inhibits the growth of LeuRS-edited defective yeast cells (D419A/Sc?leuS);
in addition, the study is the first to report that D419A/Sc?leuS cells convert some "toxic" Nva into "non-toxic" amino acids (Pro, Glu and Gln), reducing reactive oxygen clusters (ROS) and thus reducing Nva's coercion of D419A/Sc?leuS cells and protecting cells.
the work has been funded by projects of the Chinese Academy of Sciences, the Ministry of Science and Technology and the National Natural Science Foundation of China.
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