<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Somarajan SR</submitter><funding>NIA NIH HHS</funding><funding>NIAID NIH HHS</funding><funding>NCI NIH HHS</funding><pagination>1821-31</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC3013625</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>12(12)</volume><pubmed_abstract>We identified Mpn133 as a Ca(2+)-dependent cytotoxic nuclease of Mycoplasma pneumoniae. Flow cytometry analysis and immunofluorescence studies revealed the binding and internalization of recombinant Mpn133 (rMpn133) in human airway A549 cells. Amino acid sequence comparisons of Mpn133 with other mycoplasma nucleases demonstrated the presence of a unique glutamic acid-, lysine- and serine-rich region (EKS region; amino acids 72-110). Deletion of this EKS peptide (rMpn133(Δ72-110)) abrogated its binding and internalization but not its nuclease activity. The function of the EKS region in host cell trafficking and nuclear localization was reinforced by the successful delivery of EKS-conjugated mCherry protein into A549 cells. rMpn133, but not rMpn133(Δ72-110), induced apoptosis-like death in A</pubmed_abstract><journal>Cellular microbiology</journal><pubmed_title>Mycoplasma pneumoniae Mpn133 is a cytotoxic nuclease with a glutamic acid-, lysine- and serine-rich region essential for binding and internalization but not enzymatic activity.</pubmed_title><pmcid>PMC3013625</pmcid><funding_grant_id>P30 AG013319</funding_grant_id><funding_grant_id>U19 AI070412</funding_grant_id><funding_grant_id>P30 CA054174</funding_grant_id><funding_grant_id>P01 AG019316</funding_grant_id><funding_grant_id>P01 AG19316</funding_grant_id><funding_grant_id>P30 CA54174</funding_grant_id><pubmed_authors>Kannan TR</pubmed_authors><pubmed_authors>Somarajan SR</pubmed_authors><pubmed_authors>Baseman JB</pubmed_authors></additional><is_claimable>false</is_claimable><name>Mycoplasma pneumoniae Mpn133 is a cytotoxic nuclease with a glutamic acid-, lysine- and serine-rich region essential for binding and internalization but not enzymatic activity.</name><description>We identified Mpn133 as a Ca(2+)-dependent cytotoxic nuclease of Mycoplasma pneumoniae. Flow cytometry analysis and immunofluorescence studies revealed the binding and internalization of recombinant Mpn133 (rMpn133) in human airway A549 cells. Amino acid sequence comparisons of Mpn133 with other mycoplasma nucleases demonstrated the presence of a unique glutamic acid-, lysine- and serine-rich region (EKS region; amino acids 72-110). Deletion of this EKS peptide (rMpn133(Δ72-110)) abrogated its binding and internalization but not its nuclease activity. The function of the EKS region in host cell trafficking and nuclear localization was reinforced by the successful delivery of EKS-conjugated mCherry protein into A549 cells. rMpn133, but not rMpn133(Δ72-110), induced apoptosis-like death in A</description><dates><release>2010-01-01T00:00:00Z</release><publication>2010 Dec</publication><modification>2026-05-01T20:55:03.059Z</modification><creation>2019-03-27T00:37:47Z</creation></dates><accession>S-EPMC3013625</accession><cross_references><pubmed>20690923</pubmed><doi>10.1111/j.1462-5822.2010.01513.x</doi></cross_references></HashMap>