Group II Intron Protein Localization and Insertion Sites Are Affected by Polyphosphate

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dc.creatorZhao, Junhuaen
dc.creatorNiu, Weien
dc.creatorYao, Junen
dc.creatorMohr, Sabineen
dc.creatorMarcotte, Edward M.en
dc.creatorLambowitz, Alan M.en
dc.date.accessioned2013-05-28T16:59:26Zen
dc.date.available2013-05-28T16:59:26Zen
dc.date.issued2008-06-24en
dc.description.abstractMobile group II introns consist of a catalytic intron RNA and an intron-encoded protein with reverse transcriptase activity, which act together in a ribonucleoprotein particle to promote DNA integration during intron mobility. Previously, we found that the Lactococcus lactis Ll.LtrB intron-encoded protein (LtrA) expressed alone or with the intron RNA to form ribonucleoprotein particles localizes to bacterial cellular poles, potentially accounting for the intron's preferential insertion in the oriC and ter regions of the Escherichia coli chromosome. Here, by using cell microarrays and automated fluorescence microscopy to screen a transposon-insertion library, we identified five E. coli genes (gppA, uhpT, wcaK, ynbC, and zntR) whose disruption results in both an increased proportion of cells with more diffuse LtrA localization and a more uniform genomic distribution of Ll.LtrB-insertion sites. Surprisingly, we find that a common factor affecting LtrA localization in these and other disruptants is the accumulation of intracellular polyphosphate, which appears to bind LtrA and other basic proteins and delocalize them away from the poles. Our findings show that the intracellular localization of a group II intron-encoded protein is a major determinant of insertion-site preference. More generally, our results suggest that polyphosphate accumulation may provide a means of localizing proteins to different sites of action during cellular stress or entry into stationary phase, with potentially wide physiological consequences.en
dc.description.departmentCellular and Molecular Biologyen
dc.description.sponsorshipThis work was supported by National Institutes of Health R01 grants GM037949 to AML and GM076536 to EMM, Welch Foundation grants F-1607 to AML and F-1515 to EMM, and a Packard Foundation fellowship to EMM.en
dc.identifier.citationZhao J, Niu W, Yao J, Mohr S, Marcotte EM, et al. (2008) Group II Intron Protein Localization and Insertion Sites Are Affected by Polyphosphate. PLoS Biol 6(6): e150. doi:10.1371/journal.pbio.0060150en
dc.identifier.doi10.1371/journal.pbio.0060150en
dc.identifier.urihttp://hdl.handle.net/2152/20203en
dc.language.isoengen
dc.publisherPublic Library of Scienceen
dc.rightsAttribution 3.0 United Statesen
dc.rightsCC-BYen
dc.rights.urihttp://creativecommons.org/licenses/by/3.0/us/en
dc.subjectBacterial genomicsen
dc.subjectCell disruptionen
dc.subjectFluorescence microscopyen
dc.subjectGene disruptionen
dc.subjectGene targetingen
dc.subjectIntronsen
dc.subjectLibrary screeningen
dc.subjectProtein expressionen
dc.titleGroup II Intron Protein Localization and Insertion Sites Are Affected by Polyphosphateen
dc.typeArticleen

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