Unraveling the role of the enigmatic MatK maturase in chloroplast group IIA intron excision

Abstract Maturases are prokaryotic enzymes that aid self‐excision of introns in precursor RNAs and have evolutionary ties to the nuclear spliceosome. Both the mitochondria and chloroplast, due to their prokaryotic origin, encode a single intron maturase, MatR for the mitochondria and MatK for the ch...

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Main Authors: Michelle M. Barthet, Christopher L. Pierpont, Emilie‐Katherine Tavernier
Format: Article
Language:English
Published: Wiley 2020-03-01
Series:Plant Direct
Subjects:
Online Access:https://doi.org/10.1002/pld3.208
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spelling doaj-e293591f3d56439e80120fc8202c08202021-05-02T21:38:54ZengWileyPlant Direct2475-44552020-03-0143n/an/a10.1002/pld3.208Unraveling the role of the enigmatic MatK maturase in chloroplast group IIA intron excisionMichelle M. Barthet0Christopher L. Pierpont1Emilie‐Katherine Tavernier2Department of Biology Coastal Carolina University Conway SC USADepartment of Biology Coastal Carolina University Conway SC USADepartment of Biology Coastal Carolina University Conway SC USAAbstract Maturases are prokaryotic enzymes that aid self‐excision of introns in precursor RNAs and have evolutionary ties to the nuclear spliceosome. Both the mitochondria and chloroplast, due to their prokaryotic origin, encode a single intron maturase, MatR for the mitochondria and MatK for the chloroplast. MatK is proposed to aid excision of seven different chloroplast group IIA introns that reside within precursor RNAs for essential elements of chloroplast function. We have developed an in vitro activity assay to test chloroplast group IIA intron excision. Using this assay, we demonstrate self‐excision of the group IIA intron of the second intron of rps12 and the group IIA intron of rpl2. We further show that the addition of heterologously expressed MatK protein increases efficiency of group IIA intron self‐splicing for the second intron of rps12 but not the group IIA intron of rpl2. These data, to our knowledge, provide the first direct evidence of MatK’s maturase activity.https://doi.org/10.1002/pld3.208chloroplastgroup II intronintron splicingMatKmaturase
collection DOAJ
language English
format Article
sources DOAJ
author Michelle M. Barthet
Christopher L. Pierpont
Emilie‐Katherine Tavernier
spellingShingle Michelle M. Barthet
Christopher L. Pierpont
Emilie‐Katherine Tavernier
Unraveling the role of the enigmatic MatK maturase in chloroplast group IIA intron excision
Plant Direct
chloroplast
group II intron
intron splicing
MatK
maturase
author_facet Michelle M. Barthet
Christopher L. Pierpont
Emilie‐Katherine Tavernier
author_sort Michelle M. Barthet
title Unraveling the role of the enigmatic MatK maturase in chloroplast group IIA intron excision
title_short Unraveling the role of the enigmatic MatK maturase in chloroplast group IIA intron excision
title_full Unraveling the role of the enigmatic MatK maturase in chloroplast group IIA intron excision
title_fullStr Unraveling the role of the enigmatic MatK maturase in chloroplast group IIA intron excision
title_full_unstemmed Unraveling the role of the enigmatic MatK maturase in chloroplast group IIA intron excision
title_sort unraveling the role of the enigmatic matk maturase in chloroplast group iia intron excision
publisher Wiley
series Plant Direct
issn 2475-4455
publishDate 2020-03-01
description Abstract Maturases are prokaryotic enzymes that aid self‐excision of introns in precursor RNAs and have evolutionary ties to the nuclear spliceosome. Both the mitochondria and chloroplast, due to their prokaryotic origin, encode a single intron maturase, MatR for the mitochondria and MatK for the chloroplast. MatK is proposed to aid excision of seven different chloroplast group IIA introns that reside within precursor RNAs for essential elements of chloroplast function. We have developed an in vitro activity assay to test chloroplast group IIA intron excision. Using this assay, we demonstrate self‐excision of the group IIA intron of the second intron of rps12 and the group IIA intron of rpl2. We further show that the addition of heterologously expressed MatK protein increases efficiency of group IIA intron self‐splicing for the second intron of rps12 but not the group IIA intron of rpl2. These data, to our knowledge, provide the first direct evidence of MatK’s maturase activity.
topic chloroplast
group II intron
intron splicing
MatK
maturase
url https://doi.org/10.1002/pld3.208
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