Group II intron protein localization and insertion sites are affected by polyphosphate.

Mobile 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 p...

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Autores principales:	Junhua Zhao, Wei Niu, Jun Yao, Sabine Mohr, Edward M Marcotte, Alan M Lambowitz
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2008
Materias:	Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/a5a85bff1618402ba887044c0e7a1caa
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spelling	oai:doaj.org-article:a5a85bff1618402ba887044c0e7a1caa2021-11-25T05:33:18ZGroup II intron protein localization and insertion sites are affected by polyphosphate.1544-91731545-788510.1371/journal.pbio.0060150https://doaj.org/article/a5a85bff1618402ba887044c0e7a1caa2008-06-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/18593213/pdf/?tool=EBIhttps://doaj.org/toc/1544-9173https://doaj.org/toc/1545-7885Mobile 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.Junhua ZhaoWei NiuJun YaoSabine MohrEdward M MarcotteAlan M LambowitzPublic Library of Science (PLoS)articleBiology (General)QH301-705.5ENPLoS Biology, Vol 6, Iss 6, p e150 (2008)
institution	DOAJ
collection	DOAJ
language	EN
topic	Biology (General) QH301-705.5
spellingShingle	Biology (General) QH301-705.5 Junhua Zhao Wei Niu Jun Yao Sabine Mohr Edward M Marcotte Alan M Lambowitz Group II intron protein localization and insertion sites are affected by polyphosphate.
description	Mobile 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.
format	article
author	Junhua Zhao Wei Niu Jun Yao Sabine Mohr Edward M Marcotte Alan M Lambowitz
author_facet	Junhua Zhao Wei Niu Jun Yao Sabine Mohr Edward M Marcotte Alan M Lambowitz
author_sort	Junhua Zhao
title	Group II intron protein localization and insertion sites are affected by polyphosphate.
title_short	Group II intron protein localization and insertion sites are affected by polyphosphate.
title_full	Group II intron protein localization and insertion sites are affected by polyphosphate.
title_fullStr	Group II intron protein localization and insertion sites are affected by polyphosphate.
title_full_unstemmed	Group II intron protein localization and insertion sites are affected by polyphosphate.
title_sort	group ii intron protein localization and insertion sites are affected by polyphosphate.
publisher	Public Library of Science (PLoS)
publishDate	2008
url	https://doaj.org/article/a5a85bff1618402ba887044c0e7a1caa
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Group II intron protein localization and insertion sites are affected by polyphosphate.

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