Differential regulation of the accumulation of the light-harvesting chlorophyll a/b complex and ribulose bisphosphate carboxylase/oxygenase in greening pea leaves

The photoregulation of chloroplast development in pea leaves has been studied by reference to three polypeptides and their mRNAs. The polypeptides were the large subunit (LSU) and the small subunit (SSU) of ribulose 1,5‐bisphosphate carbox‐ylase/oxygenase (RUBISCO), and the light‐harvesting chloroph...

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Veröffentlicht in:Journal of cellular biochemistry 1984, Vol.25 (1), p.1-13
Hauptverfasser: Bennett, John, Jenkins, Gareth I., Hartley, Martin R.
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description The photoregulation of chloroplast development in pea leaves has been studied by reference to three polypeptides and their mRNAs. The polypeptides were the large subunit (LSU) and the small subunit (SSU) of ribulose 1,5‐bisphosphate carbox‐ylase/oxygenase (RUBISCO), and the light‐harvesting chlorophyll a/b protein (LHCP). The polypeptides were assayed by a sensitive radioimmune assay, and the mRNAs were assayed by hybridization to cloned DNA probes. LSU, LSU mRNA, and LHCP mRNA were detectable in etiolated seedlings but LHCP, SSU, and SSU mRNA were at or below the limit of detection. During the first 48 hr of de‐etiolation under continuous white light, the mRNAs for LSU, SSU, and LHCP increased in concentration per apical bud by about 40‐fold, at least 200‐fold, and about 25‐fold, respectively, while the total RNA content per apical bud increased only 3.5‐fold. In the same period, the LSU, SSU, and LHCP contents per bud increased at least 60‐, 100‐, and 200‐fold, respectively. The LHCP increased steadily in concentration during de‐etiolation, whereas the accumulation LSU, SSU, and SSU mRNA showed a 24‐hr lag. The accumulation of SSU, SSU mRNA, and LHCP mRNA showed classical red/far‐red reversibility, indicating the involvement of phytochrome in the regulatory mechanism. LSU and LSU mRNA were induced equally well by red and far‐red light. The LHCP failed to accumulate except under continuous illumination. These results indicate that the accumulation of SSU is controlled largely through the steady‐state level of its mRNA, which is in turn almost totally dependent on light as an inducer and on phytochrome as one of the photoreceptors. The accumulation of LSU is largely but not totally determined by the level of its mRNA, which appears to be under strong photoregulation, which has yet to be shown to involve phytochrome. Phytochrome is involved in the regulation of LHCP mRNA levels but substantial levels of the mRNA also occur in the dark. LHCP accumulation is not primarily governed by the levels of LHCP mRNA but by posttranslational stabilization in which chlorophyll synthesis plays a necessary but not sufficient role.
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The polypeptides were the large subunit (LSU) and the small subunit (SSU) of ribulose 1,5‐bisphosphate carbox‐ylase/oxygenase (RUBISCO), and the light‐harvesting chlorophyll a/b protein (LHCP). The polypeptides were assayed by a sensitive radioimmune assay, and the mRNAs were assayed by hybridization to cloned DNA probes. LSU, LSU mRNA, and LHCP mRNA were detectable in etiolated seedlings but LHCP, SSU, and SSU mRNA were at or below the limit of detection. During the first 48 hr of de‐etiolation under continuous white light, the mRNAs for LSU, SSU, and LHCP increased in concentration per apical bud by about 40‐fold, at least 200‐fold, and about 25‐fold, respectively, while the total RNA content per apical bud increased only 3.5‐fold. In the same period, the LSU, SSU, and LHCP contents per bud increased at least 60‐, 100‐, and 200‐fold, respectively. The LHCP increased steadily in concentration during de‐etiolation, whereas the accumulation LSU, SSU, and SSU mRNA showed a 24‐hr lag. The accumulation of SSU, SSU mRNA, and LHCP mRNA showed classical red/far‐red reversibility, indicating the involvement of phytochrome in the regulatory mechanism. LSU and LSU mRNA were induced equally well by red and far‐red light. The LHCP failed to accumulate except under continuous illumination. These results indicate that the accumulation of SSU is controlled largely through the steady‐state level of its mRNA, which is in turn almost totally dependent on light as an inducer and on phytochrome as one of the photoreceptors. The accumulation of LSU is largely but not totally determined by the level of its mRNA, which appears to be under strong photoregulation, which has yet to be shown to involve phytochrome. Phytochrome is involved in the regulation of LHCP mRNA levels but substantial levels of the mRNA also occur in the dark. LHCP accumulation is not primarily governed by the levels of LHCP mRNA but by posttranslational stabilization in which chlorophyll synthesis plays a necessary but not sufficient role.</description><identifier>ISSN: 0730-2312</identifier><identifier>EISSN: 1097-4644</identifier><identifier>DOI: 10.1002/jcb.240250102</identifier><identifier>PMID: 6470048</identifier><identifier>CODEN: JCEBD5</identifier><language>eng</language><publisher>Hoboken: Wiley Subscription Services, Inc., A Wiley Company</publisher><subject>Biological and medical sciences ; Cell structures and functions ; Chlorophyll - biosynthesis ; Chlorophyll - genetics ; chlorophyll a/b protein ; chloroplast ; Chloroplast, photosynthetic membrane and photosynthesis ; Chloroplasts - metabolism ; Fabaceae ; Fundamental and applied biological sciences. Psychology ; Gene Expression Regulation ; Light ; light-harvesting chlorophyll a/b complex ; light-harvesting proteins ; Molecular and cellular biology ; mRNA ; mRNA levels ; oxygenase ; photosynthesis ; Phytochrome - genetics ; Pisum sativum ; Plants, Medicinal ; regulation of biosynthesis ; ribulose bisphosphate carboxylase ; Ribulose-Bisphosphate Carboxylase - biosynthesis ; Ribulose-Bisphosphate Carboxylase - genetics ; ribulosebisphosphate carboxylase ; RNA, Messenger - genetics</subject><ispartof>Journal of cellular biochemistry, 1984, Vol.25 (1), p.1-13</ispartof><rights>Copyright © 1984 Alan R. 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Cell. Biochem</addtitle><description>The photoregulation of chloroplast development in pea leaves has been studied by reference to three polypeptides and their mRNAs. The polypeptides were the large subunit (LSU) and the small subunit (SSU) of ribulose 1,5‐bisphosphate carbox‐ylase/oxygenase (RUBISCO), and the light‐harvesting chlorophyll a/b protein (LHCP). The polypeptides were assayed by a sensitive radioimmune assay, and the mRNAs were assayed by hybridization to cloned DNA probes. LSU, LSU mRNA, and LHCP mRNA were detectable in etiolated seedlings but LHCP, SSU, and SSU mRNA were at or below the limit of detection. During the first 48 hr of de‐etiolation under continuous white light, the mRNAs for LSU, SSU, and LHCP increased in concentration per apical bud by about 40‐fold, at least 200‐fold, and about 25‐fold, respectively, while the total RNA content per apical bud increased only 3.5‐fold. In the same period, the LSU, SSU, and LHCP contents per bud increased at least 60‐, 100‐, and 200‐fold, respectively. The LHCP increased steadily in concentration during de‐etiolation, whereas the accumulation LSU, SSU, and SSU mRNA showed a 24‐hr lag. The accumulation of SSU, SSU mRNA, and LHCP mRNA showed classical red/far‐red reversibility, indicating the involvement of phytochrome in the regulatory mechanism. LSU and LSU mRNA were induced equally well by red and far‐red light. The LHCP failed to accumulate except under continuous illumination. These results indicate that the accumulation of SSU is controlled largely through the steady‐state level of its mRNA, which is in turn almost totally dependent on light as an inducer and on phytochrome as one of the photoreceptors. The accumulation of LSU is largely but not totally determined by the level of its mRNA, which appears to be under strong photoregulation, which has yet to be shown to involve phytochrome. Phytochrome is involved in the regulation of LHCP mRNA levels but substantial levels of the mRNA also occur in the dark. LHCP accumulation is not primarily governed by the levels of LHCP mRNA but by posttranslational stabilization in which chlorophyll synthesis plays a necessary but not sufficient role.</description><subject>Biological and medical sciences</subject><subject>Cell structures and functions</subject><subject>Chlorophyll - biosynthesis</subject><subject>Chlorophyll - genetics</subject><subject>chlorophyll a/b protein</subject><subject>chloroplast</subject><subject>Chloroplast, photosynthetic membrane and photosynthesis</subject><subject>Chloroplasts - metabolism</subject><subject>Fabaceae</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene Expression Regulation</subject><subject>Light</subject><subject>light-harvesting chlorophyll a/b complex</subject><subject>light-harvesting proteins</subject><subject>Molecular and cellular biology</subject><subject>mRNA</subject><subject>mRNA levels</subject><subject>oxygenase</subject><subject>photosynthesis</subject><subject>Phytochrome - genetics</subject><subject>Pisum sativum</subject><subject>Plants, Medicinal</subject><subject>regulation of biosynthesis</subject><subject>ribulose bisphosphate carboxylase</subject><subject>Ribulose-Bisphosphate Carboxylase - biosynthesis</subject><subject>Ribulose-Bisphosphate Carboxylase - genetics</subject><subject>ribulosebisphosphate carboxylase</subject><subject>RNA, Messenger - genetics</subject><issn>0730-2312</issn><issn>1097-4644</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1984</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU1vFDEMhkcIVErhyBEpB8Rtus7HfB1hgQKqihAfPUaerGcnJTuZJjOw-3f4paTa1QpxgEPkyH782tabZU85nHMAsbgx7blQIArgIO5lpxyaKlelUvezU6gk5EJy8TB7FOMNADSNFCfZSakqAFWfZr9e266jQMNk0bFA69nhZP3AfMemnhgaM2_-yjm77qe8x_CD4mSHNTO988GP_c45houWGb8ZHW0ZDisWbDs7H4m1No69Tw8nYgZD67c7h5EWKa5pSD9mB7YORMOd5kjIHGEa8Th70KGL9OQQz7Kvb998Wb7LLz9evF--vMyNkkrkpjaGsICyq2Qjal5XXUoBio4XvJOr0pTYtKIu6xp4C60SyAtYqbIDIaVs5Vn2Yq87Bn87p9P0xkZDzuFAfo665gIKIdR_Qa5EKROdwHwPmuBjDNTpMdgNhp3moO_M08k8fTQv8c8OwnO7odWRPriV6s8PdYwGXRdwMDYesbopuKqqhFV77Kd1tPv3TP1h-erPBQ4L2zjR9tiJ4bsuK1kV-vrqQtfX_Nun5ecrzeVv5yLERA</recordid><startdate>1984</startdate><enddate>1984</enddate><creator>Bennett, John</creator><creator>Jenkins, Gareth I.</creator><creator>Hartley, Martin R.</creator><general>Wiley Subscription Services, Inc., A Wiley Company</general><general>Wiley-Liss</general><scope>BSCLL</scope><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7TM</scope><scope>8FD</scope><scope>FR3</scope><scope>M7Z</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>1984</creationdate><title>Differential regulation of the accumulation of the light-harvesting chlorophyll a/b complex and ribulose bisphosphate carboxylase/oxygenase in greening pea leaves</title><author>Bennett, John ; Jenkins, Gareth I. ; Hartley, Martin R.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4342-c8ccea506f73928187fc8c0a2f151f3d6c6a9b2868801b0b42a150d46f02333b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1984</creationdate><topic>Biological and medical sciences</topic><topic>Cell structures and functions</topic><topic>Chlorophyll - biosynthesis</topic><topic>Chlorophyll - genetics</topic><topic>chlorophyll a/b protein</topic><topic>chloroplast</topic><topic>Chloroplast, photosynthetic membrane and photosynthesis</topic><topic>Chloroplasts - metabolism</topic><topic>Fabaceae</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gene Expression Regulation</topic><topic>Light</topic><topic>light-harvesting chlorophyll a/b complex</topic><topic>light-harvesting proteins</topic><topic>Molecular and cellular biology</topic><topic>mRNA</topic><topic>mRNA levels</topic><topic>oxygenase</topic><topic>photosynthesis</topic><topic>Phytochrome - genetics</topic><topic>Pisum sativum</topic><topic>Plants, Medicinal</topic><topic>regulation of biosynthesis</topic><topic>ribulose bisphosphate carboxylase</topic><topic>Ribulose-Bisphosphate Carboxylase - biosynthesis</topic><topic>Ribulose-Bisphosphate Carboxylase - genetics</topic><topic>ribulosebisphosphate carboxylase</topic><topic>RNA, Messenger - genetics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bennett, John</creatorcontrib><creatorcontrib>Jenkins, Gareth I.</creatorcontrib><creatorcontrib>Hartley, Martin R.</creatorcontrib><collection>Istex</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Nucleic Acids Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 1</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of cellular biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Bennett, John</au><au>Jenkins, Gareth I.</au><au>Hartley, Martin R.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Differential regulation of the accumulation of the light-harvesting chlorophyll a/b complex and ribulose bisphosphate carboxylase/oxygenase in greening pea leaves</atitle><jtitle>Journal of cellular biochemistry</jtitle><addtitle>J. Cell. Biochem</addtitle><date>1984</date><risdate>1984</risdate><volume>25</volume><issue>1</issue><spage>1</spage><epage>13</epage><pages>1-13</pages><issn>0730-2312</issn><eissn>1097-4644</eissn><coden>JCEBD5</coden><abstract>The photoregulation of chloroplast development in pea leaves has been studied by reference to three polypeptides and their mRNAs. The polypeptides were the large subunit (LSU) and the small subunit (SSU) of ribulose 1,5‐bisphosphate carbox‐ylase/oxygenase (RUBISCO), and the light‐harvesting chlorophyll a/b protein (LHCP). The polypeptides were assayed by a sensitive radioimmune assay, and the mRNAs were assayed by hybridization to cloned DNA probes. LSU, LSU mRNA, and LHCP mRNA were detectable in etiolated seedlings but LHCP, SSU, and SSU mRNA were at or below the limit of detection. During the first 48 hr of de‐etiolation under continuous white light, the mRNAs for LSU, SSU, and LHCP increased in concentration per apical bud by about 40‐fold, at least 200‐fold, and about 25‐fold, respectively, while the total RNA content per apical bud increased only 3.5‐fold. In the same period, the LSU, SSU, and LHCP contents per bud increased at least 60‐, 100‐, and 200‐fold, respectively. The LHCP increased steadily in concentration during de‐etiolation, whereas the accumulation LSU, SSU, and SSU mRNA showed a 24‐hr lag. The accumulation of SSU, SSU mRNA, and LHCP mRNA showed classical red/far‐red reversibility, indicating the involvement of phytochrome in the regulatory mechanism. LSU and LSU mRNA were induced equally well by red and far‐red light. The LHCP failed to accumulate except under continuous illumination. These results indicate that the accumulation of SSU is controlled largely through the steady‐state level of its mRNA, which is in turn almost totally dependent on light as an inducer and on phytochrome as one of the photoreceptors. The accumulation of LSU is largely but not totally determined by the level of its mRNA, which appears to be under strong photoregulation, which has yet to be shown to involve phytochrome. Phytochrome is involved in the regulation of LHCP mRNA levels but substantial levels of the mRNA also occur in the dark. LHCP accumulation is not primarily governed by the levels of LHCP mRNA but by posttranslational stabilization in which chlorophyll synthesis plays a necessary but not sufficient role.</abstract><cop>Hoboken</cop><pub>Wiley Subscription Services, Inc., A Wiley Company</pub><pmid>6470048</pmid><doi>10.1002/jcb.240250102</doi><tpages>13</tpages></addata></record>
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source MEDLINE; Wiley Online Library Journals Frontfile Complete
subjects Biological and medical sciences
Cell structures and functions
Chlorophyll - biosynthesis
Chlorophyll - genetics
chlorophyll a/b protein
chloroplast
Chloroplast, photosynthetic membrane and photosynthesis
Chloroplasts - metabolism
Fabaceae
Fundamental and applied biological sciences. Psychology
Gene Expression Regulation
Light
light-harvesting chlorophyll a/b complex
light-harvesting proteins
Molecular and cellular biology
mRNA
mRNA levels
oxygenase
photosynthesis
Phytochrome - genetics
Pisum sativum
Plants, Medicinal
regulation of biosynthesis
ribulose bisphosphate carboxylase
Ribulose-Bisphosphate Carboxylase - biosynthesis
Ribulose-Bisphosphate Carboxylase - genetics
ribulosebisphosphate carboxylase
RNA, Messenger - genetics
title Differential regulation of the accumulation of the light-harvesting chlorophyll a/b complex and ribulose bisphosphate carboxylase/oxygenase in greening pea leaves
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