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UMP kinase activity is involved in proper chloroplast development in rice

Isolation of leaf-color mutants is important in understanding the mechanisms of chloroplast biogenesis and development. In this study, we identified and characterized a rice (Oryza sativa) mutant, yellow leaf 2 (yl2), exhibiting pale yellow leaves with a few longitudinal white stripes at the early s...

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Autores principales: Chen, Fei, Dong, Guojun, Ma, Xiaohui, Wang, Fang, Zhang, Yanli, Xiong, Erhui, Wu, Jiahuan, Wang, Huizhong, Qian, Qian, Wu, Limin, Yu, Yanchun
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer Netherlands 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5999181/
https://www.ncbi.nlm.nih.gov/pubmed/29392476
http://dx.doi.org/10.1007/s11120-017-0477-5
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author Chen, Fei
Dong, Guojun
Ma, Xiaohui
Wang, Fang
Zhang, Yanli
Xiong, Erhui
Wu, Jiahuan
Wang, Huizhong
Qian, Qian
Wu, Limin
Yu, Yanchun
author_facet Chen, Fei
Dong, Guojun
Ma, Xiaohui
Wang, Fang
Zhang, Yanli
Xiong, Erhui
Wu, Jiahuan
Wang, Huizhong
Qian, Qian
Wu, Limin
Yu, Yanchun
author_sort Chen, Fei
collection PubMed
description Isolation of leaf-color mutants is important in understanding the mechanisms of chloroplast biogenesis and development. In this study, we identified and characterized a rice (Oryza sativa) mutant, yellow leaf 2 (yl2), exhibiting pale yellow leaves with a few longitudinal white stripes at the early seedling stage then gradually turning yellow. Genetic analyses revealed that YL2 encodes a thylakoid membrane-localized protein with significant sequence similarity to UMP kinase proteins in prokaryotes and eukaryotes. Prokaryotic UMP kinase activity was subsequently confirmed, with YL2 deficiency causing a significant reduction in chlorophyll accumulation and photochemical efficiency. Moreover, YL2 is also light dependent and preferentially expressed in green tissues. Chloroplast development was abnormal in the yl2 mutant, possibly due to reduced accumulation of thylakoid membranes and a lack of normal stroma lamellae. 2D Blue-Native SDS-PAGE and immunoblot analyses revealed a reduction in several subunits of photosynthetic complexes, in particular, the AtpB subunit of ATP synthase, while mRNA levels of corresponding genes were unchanged or increased compared with the wild type. In addition, we observed a significant decrease (ca. 36.3%) in cpATPase activity in the yl2 mutant compared with the wild type. Taken together, our results suggest that UMP kinase activity plays an essential role in chloroplast development and regulating cpATPase biogenesis in rice. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (10.1007/s11120-017-0477-5) contains supplementary material, which is available to authorized users.
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spelling pubmed-59991812018-06-28 UMP kinase activity is involved in proper chloroplast development in rice Chen, Fei Dong, Guojun Ma, Xiaohui Wang, Fang Zhang, Yanli Xiong, Erhui Wu, Jiahuan Wang, Huizhong Qian, Qian Wu, Limin Yu, Yanchun Photosynth Res Original Article Isolation of leaf-color mutants is important in understanding the mechanisms of chloroplast biogenesis and development. In this study, we identified and characterized a rice (Oryza sativa) mutant, yellow leaf 2 (yl2), exhibiting pale yellow leaves with a few longitudinal white stripes at the early seedling stage then gradually turning yellow. Genetic analyses revealed that YL2 encodes a thylakoid membrane-localized protein with significant sequence similarity to UMP kinase proteins in prokaryotes and eukaryotes. Prokaryotic UMP kinase activity was subsequently confirmed, with YL2 deficiency causing a significant reduction in chlorophyll accumulation and photochemical efficiency. Moreover, YL2 is also light dependent and preferentially expressed in green tissues. Chloroplast development was abnormal in the yl2 mutant, possibly due to reduced accumulation of thylakoid membranes and a lack of normal stroma lamellae. 2D Blue-Native SDS-PAGE and immunoblot analyses revealed a reduction in several subunits of photosynthetic complexes, in particular, the AtpB subunit of ATP synthase, while mRNA levels of corresponding genes were unchanged or increased compared with the wild type. In addition, we observed a significant decrease (ca. 36.3%) in cpATPase activity in the yl2 mutant compared with the wild type. Taken together, our results suggest that UMP kinase activity plays an essential role in chloroplast development and regulating cpATPase biogenesis in rice. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (10.1007/s11120-017-0477-5) contains supplementary material, which is available to authorized users. Springer Netherlands 2018-02-01 2018 /pmc/articles/PMC5999181/ /pubmed/29392476 http://dx.doi.org/10.1007/s11120-017-0477-5 Text en © The Author(s) 2018 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.
spellingShingle Original Article
Chen, Fei
Dong, Guojun
Ma, Xiaohui
Wang, Fang
Zhang, Yanli
Xiong, Erhui
Wu, Jiahuan
Wang, Huizhong
Qian, Qian
Wu, Limin
Yu, Yanchun
UMP kinase activity is involved in proper chloroplast development in rice
title UMP kinase activity is involved in proper chloroplast development in rice
title_full UMP kinase activity is involved in proper chloroplast development in rice
title_fullStr UMP kinase activity is involved in proper chloroplast development in rice
title_full_unstemmed UMP kinase activity is involved in proper chloroplast development in rice
title_short UMP kinase activity is involved in proper chloroplast development in rice
title_sort ump kinase activity is involved in proper chloroplast development in rice
topic Original Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5999181/
https://www.ncbi.nlm.nih.gov/pubmed/29392476
http://dx.doi.org/10.1007/s11120-017-0477-5
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