[Objectives]To clone the sucC gene of Vibrio alginolyticus strain HY9901 and conduct the bioinformatics analysis.[Methods]Based on the sucC gene of V.alginolyticus strain HY9901,specific primers were designed to ampli...[Objectives]To clone the sucC gene of Vibrio alginolyticus strain HY9901 and conduct the bioinformatics analysis.[Methods]Based on the sucC gene of V.alginolyticus strain HY9901,specific primers were designed to amplify the full length sequence by PCR and make further analysis.[Results]The theoretical molecular weight of SucC protein was about 41528.45 Da,and the full length was 1167 bp,encoding 388 amino acids.It has no signal peptide and transmembrane region,and has a variety of functional sites.It is predicted that it is mainly located in the cytoplasm,and the ubiquitin and lactate modification sites overlap,and it has high gene homology with Vibrio parahaemolyticus.Theα-helix,random coil and extended strand are the main secondary structures.The similarity between the constructed three-level structure model and the template is high.[Conclusions]This study reveals the structural characteristics and functional potential of SucC protein,and provides a theoretical basis for the study of drug resistance mechanism and prevention strategies.展开更多
Emerging evidence suggests that amino acids dictate the effector functions of immune cells;however, whether and how phenylalanine(Phe) orchestrates the polarization of macrophages is not understood. Here, we determine...Emerging evidence suggests that amino acids dictate the effector functions of immune cells;however, whether and how phenylalanine(Phe) orchestrates the polarization of macrophages is not understood. Here, we determined that Phe attenuated lipopolysaccharide(LPS) and P. multocida serotype A strain CQ2(PmCQ2) infection-induced inflammation in vivo. Furthermore, we demonstrated that Phe inhibited the production of interleukin(IL)-1β and tumor necrosis factor(TNF)-α in proinflammatory(M1) macrophages. Phe reprogrammed the transcriptomic and metabolic profiles and enhanced oxidative phosphorylation in M1 macrophages, which reduced the activation of caspase-1. Notably, the valine-succinyl-CoA axis played a critical role in Phe-mediated inhibition of IL-1β production in M1 macrophages. Taken together, our findings suggest that manipulating the valine-succinyl-CoA axis provides a potential target for preventing and/or treating macrophage-related diseases.展开更多
Lysine succinylation is a naturally occurring post-translational modification(PTM)that regulates the stability and function of proteins.It can be regulated by enzymes such as SIRT5 and SIRT7.Recently,the effect and si...Lysine succinylation is a naturally occurring post-translational modification(PTM)that regulates the stability and function of proteins.It can be regulated by enzymes such as SIRT5 and SIRT7.Recently,the effect and significance of lysine succinylation in cancer and its implication in immunity have been extensively explored.Lysine succinylation is involved in the malignant phenotype of cancer cells.Abnormal regulation of lysine succinylation occurs in different cancers,and inhibitors targeting lysine succinylation regulatory enzymes can be used as potential anti-cancer strategies.Therefore,this review focused on the target protein lysine succinylation and its functions in cancer and immunity,in order to provide a reference for finding more potential clinical cancer targets in the future.展开更多
Lysine succinylation(Ksucc),defined as a transfer of a succinyl group to a lysine residue of a protein,is a newly identified protein post-translational modification^1-3.This chemical modification is reversible,dynamic...Lysine succinylation(Ksucc),defined as a transfer of a succinyl group to a lysine residue of a protein,is a newly identified protein post-translational modification^1-3.This chemical modification is reversible,dynamic,and evolutionarily conserved^4 where it has been comprehensively studied in both bacterial and mammalian cells^5-7.Numerous proteins involved in the regulation of various cellular and biological processes have been shown to be heavily succinylated^5-7.Emerging clinical data provides evidence that dysregulation of Ksucc is correlated with the development of several diseases,including cardiovascular diseases and cancer^7-9.Therefore,an in-depth understanding of Ksucc and its regulation is important not only for understanding its physiological function but also for developing drug therapies and targeted agents for these diseases.In this review,we highlight some of the recent advances in understanding the role of Ksucc and desuccinylation under physiological and pathological conditions.展开更多
基金Supported by National Natural Science Foundation of China(32073015)Graduate Education Innovation Program of Guangdong Province(YJYH[2022]1)+1 种基金Undergraduate Innovation and Entrepreneurship Training Program of Guangdong Ocean University(CXXL2024007)Undergraduate Innovation Team of Guangdong Ocean University(CCTD201802).
文摘[Objectives]To clone the sucC gene of Vibrio alginolyticus strain HY9901 and conduct the bioinformatics analysis.[Methods]Based on the sucC gene of V.alginolyticus strain HY9901,specific primers were designed to amplify the full length sequence by PCR and make further analysis.[Results]The theoretical molecular weight of SucC protein was about 41528.45 Da,and the full length was 1167 bp,encoding 388 amino acids.It has no signal peptide and transmembrane region,and has a variety of functional sites.It is predicted that it is mainly located in the cytoplasm,and the ubiquitin and lactate modification sites overlap,and it has high gene homology with Vibrio parahaemolyticus.Theα-helix,random coil and extended strand are the main secondary structures.The similarity between the constructed three-level structure model and the template is high.[Conclusions]This study reveals the structural characteristics and functional potential of SucC protein,and provides a theoretical basis for the study of drug resistance mechanism and prevention strategies.
基金supported by the National Natural Science Foundation of China (32225047,31922079)the Laboratory of Lingnan Modern Agriculture Project (NT2021005)。
文摘Emerging evidence suggests that amino acids dictate the effector functions of immune cells;however, whether and how phenylalanine(Phe) orchestrates the polarization of macrophages is not understood. Here, we determined that Phe attenuated lipopolysaccharide(LPS) and P. multocida serotype A strain CQ2(PmCQ2) infection-induced inflammation in vivo. Furthermore, we demonstrated that Phe inhibited the production of interleukin(IL)-1β and tumor necrosis factor(TNF)-α in proinflammatory(M1) macrophages. Phe reprogrammed the transcriptomic and metabolic profiles and enhanced oxidative phosphorylation in M1 macrophages, which reduced the activation of caspase-1. Notably, the valine-succinyl-CoA axis played a critical role in Phe-mediated inhibition of IL-1β production in M1 macrophages. Taken together, our findings suggest that manipulating the valine-succinyl-CoA axis provides a potential target for preventing and/or treating macrophage-related diseases.
基金supported by Youth Wan Jiang Scholar of Anhui Province,China(No.DT2100001172)Beijing Xisike Clinical Oncology Research Foundation(China)(No.Y-HR2020MS-0156).
文摘Lysine succinylation is a naturally occurring post-translational modification(PTM)that regulates the stability and function of proteins.It can be regulated by enzymes such as SIRT5 and SIRT7.Recently,the effect and significance of lysine succinylation in cancer and its implication in immunity have been extensively explored.Lysine succinylation is involved in the malignant phenotype of cancer cells.Abnormal regulation of lysine succinylation occurs in different cancers,and inhibitors targeting lysine succinylation regulatory enzymes can be used as potential anti-cancer strategies.Therefore,this review focused on the target protein lysine succinylation and its functions in cancer and immunity,in order to provide a reference for finding more potential clinical cancer targets in the future.
基金We apologize to any authors whose work could not be included owing to space limitations.This work was supported in part by NIH R01 CA225680-01(T.H.)Research Scholar Grant(RSG-19-076-01-TBE)from the American Cancer Society(T.H.)Career Catalyst Research funding(CCR14300798)from the Susan G.Komen Foundation(T.H.),the Eagles Cancer Research Fund(T.H.),a Team Science Platform Award from the Mayo Clinic Center for Biomedical Discovery(T.H.),the Developmental Therapeutics Program from the Mayo Clinic Cancer Center(T.H.),and the Mayo Clinic Breast SPORE P50CA 116201-10(T.H.).E.K.W.was supported by a predoctoral fellowship from the Mayo Foundation for Education and Research.
文摘Lysine succinylation(Ksucc),defined as a transfer of a succinyl group to a lysine residue of a protein,is a newly identified protein post-translational modification^1-3.This chemical modification is reversible,dynamic,and evolutionarily conserved^4 where it has been comprehensively studied in both bacterial and mammalian cells^5-7.Numerous proteins involved in the regulation of various cellular and biological processes have been shown to be heavily succinylated^5-7.Emerging clinical data provides evidence that dysregulation of Ksucc is correlated with the development of several diseases,including cardiovascular diseases and cancer^7-9.Therefore,an in-depth understanding of Ksucc and its regulation is important not only for understanding its physiological function but also for developing drug therapies and targeted agents for these diseases.In this review,we highlight some of the recent advances in understanding the role of Ksucc and desuccinylation under physiological and pathological conditions.
