ArticleArchives of biochemistry and biophysics2003
Expression and purification of recombinant tristetraprolin that can bind to tumor necrosis factor-alpha mRNA and serve as a substrate for mitogen-activated protein kinases.
Article in Archives of biochemistry and biophysics, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed, 80 citations in OpenAlex.
- GLA-3 mediates the heat shock response in Caenorhabditis elegans germ cells: A key role for the tristetraprolin (TTP) family.PloS one · 2026Article
- Tumor-intrinsic CDC42BPB confers resistance to anti-PD-1 immune checkpoint blockade in breast cancer.Molecular therapy : the journal of the American Society of Gene Therapy · 2024Article
- Post-transcriptional regulation of BIRC5/survivin expression and induction of apoptosis in breast cancer cells by tristetraprolin.RNA biology · 2024Article
- Cottonseed extracts regulate gene expression in human colon cancer cells.Scientific reports · 2022Article
- Regulation of CCR4-NOT complex deadenylase activity and cellular responses by MK2-dependent phosphorylation of CNOT2.RNA biology · 2022Article
- Long-Lasting Stable Expression of Human LL-37 Antimicrobial Peptide in Transgenic Barley Plants.Antibiotics (Basel, Switzerland) · 2021Article
- Gossypol decreased cell viability and down-regulated the expression of a number of genes in human colon cancer cells.Scientific reports · 2021Article
- Destabilization of NOXA mRNA as a common resistance mechanism to targeted therapies.Nature communications · 2019Article
- The tandem zinc finger RNA binding domain of members of the tristetraprolin protein family.Wiley interdisciplinary reviews. RNA · 2019Review
- Roles of Tristetraprolin in Tumorigenesis.International journal of molecular sciences · 2018Review
- Article
- The control of inflammation via the phosphorylation and dephosphorylation of tristetraprolin: a tale of two phosphatases.Biochemical Society transactions · 2016Review
- Polyubiquitinated tristetraprolin protects from TNF-induced, caspase-mediated apoptosis.The Journal of biological chemistry · 2014Article
- Identification of a major phosphopeptide in human tristetraprolin by phosphopeptide mapping and mass spectrometry.PloS one · 2014Article
- Multiple functions of tristetraprolin/TIS11 RNA-binding proteins in the regulation of mRNA biogenesis and degradation.Cellular and molecular life sciences : CMLS · 2013Review
- Developmental regulation of diacylglycerol acyltransferase family gene expression in tung tree tissues.PloS one · 2013Article
- Expression and purification of recombinant tung tree diacylglycerol acyltransferase 2.Applied microbiology and biotechnology · 2012Article
- The requirement of c-Jun N-terminal kinase 2 in regulation of hypoxia-inducing factor-1α mRNA stability.The Journal of biological chemistry · 2012Article
- The role of tristetraprolin in cancer and inflammation.Frontiers in bioscience (Landmark edition) · 2012Review
- A molecular mechanism for TNF-α-mediated downregulation of B cell responses.Journal of immunology (Baltimore, Md. : 1950) · 2012Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Tristetraprolin (TTP) is an mRNA-binding protein, but studies of this interaction have been difficult due to problems with the purification of recombinant TTP. In the present study, we expressed human and mouse TTP as glutathione S-transferase and maltose-binding protein (MBP) fusion proteins in Escherichia coli, and purified them by affinity resins and Mono Q chromatography. TTP cleaved from the fusion protein was identified by immunoblotting, MALDI-MS, and protein sequencing, and was further purified to homogeneity by continuous-elution SDS-gel electrophoresis. Purified recombinant TTP bound to the AU-rich element of tumor necrosis factor-alpha (TNFalpha) mRNA and this binding was dependent on Zn(2+). Results from sizing columns suggested that the active species might be in the form of an oligomer of MBP-TTP. Recombinant TTP was phosphorylated by three members of the mitogen-activated protein (MAP) kinase family, p42, p38, and JNK, with half-maximal phosphorylation occurring at approximately 0.5, 0.25, and 0.25 microM protein, respectively. Phosphorylation by these kinases did not appear to affect the ability of TTP to bind to TNFalpha mRNA under the assay conditions. This study describes a procedure for purifying nonfusion protein TTP to homogeneity, demonstrates that TTP's RNA-binding activity is zinc dependent, and that TTP can be phosphorylated by JNK as well as by the other members of the greater MAP kinase family.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.