Dataset Information

To functionally investigate the manner that UBQLN1 regulate mitochondria function,we searched for the UBQLN1-interacting proteins,we first conducted LC-MS with 3Flag-UBQLN1 cell line

ABSTRACT: To functionally investigate the manner that UBQLN1 regulatr mitochondria function,we searched for UBQLN1-interacting proteins,we conduct LC-MS with 3flag-UBQLN1 cell line

INSTRUMENT(S): Q Exactive

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture

SUBMITTER: shuang Zhao

LAB HEAD: zhao shuang

PROVIDER: PXD036634 | Pride | 2024-07-03

REPOSITORIES: Pride

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Publications

UBQLN1 links proteostasis and mitochondria function to telomere maintenance in human embryonic stem cells.

Zhao Shuang S Li Jie J Duan Songqi S Liu Chang C Wang Hua H Lu Jiangtao J Zhao Nannan N Sheng Xiaoyan X Wu Yiwei Y Li Yanjun Y Sun Baofa B Liu Lin L

Stem cell research & therapy 20240621 1

<h4>Background</h4>Telomeres consist of repetitive DNA sequences at the chromosome ends to protect chromosomal stability, and primarily maintained by telomerase or occasionally by alternative telomere lengthening of telomeres (ALT) through recombination-based mechanisms. Additional mechanisms that may regulate telomere maintenance remain to be explored. Simultaneous measurement of telomere length and transcriptome in the same human embryonic stem cell (hESC) revealed that mRNA expression levels ...[more]

PMID: 38902824

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Project description:BackgroundSerine protease inhibitors act as modulators of serine proteases, playing important roles in protecting animal toxin peptides from degradation. However, all known serine protease inhibitors discovered thus far from animal venom belong to the Kunitz-type subfamily, and whether there are other novel types of protease inhibitors in animal venom remains unclear.Principal findingsHere, by screening scorpion venom gland cDNA libraries, we identified the first Ascaris-type animal toxin family, which contains four members: Scorpiops jendeki Ascaris-type protease inhibitor (SjAPI), Scorpiops jendeki Ascaris-type protease inhibitor 2 (SjAPI-2), Chaerilus tricostatus Ascaris-type protease inhibitor (CtAPI), and Buthus martensii Ascaris-type protease inhibitor (BmAPI). The detailed characterization of Ascaris-type peptide SjAPI from the venom gland of scorpion Scorpiops jendeki was carried out. The mature peptide of SjAPI contains 64 residues and possesses a classical Ascaris-type cysteine framework reticulated by five disulfide bridges, different from all known protease inhibitors from venomous animals. Enzyme and inhibitor reaction kinetics experiments showed that recombinant SjAPI was a dual function peptide with ?-chymotrypsin- and elastase-inhibiting properties. Recombinant SjAPI inhibited ?-chymotrypsin with a Ki of 97.1 nM and elastase with a Ki of 3.7 ?M, respectively. Bioinformatics analyses and chimera experiments indicated that SjAPI contained the unique short side chain functional residues "AAV" and might be a useful template to produce new serine protease inhibitors.Conclusions/significanceTo our knowledge, SjAPI is the first functionally characterized animal toxin peptide with an Ascaris-type fold. The structural and functional diversity of animal toxins with protease-inhibiting properties suggested that bioactive peptides from animal venom glands might be a new source of protease inhibitors, which will accelerate the development of diagnostic and therapeutic agents for human diseases that target diverse proteases.

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