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Chloroplast precursor proteins compete to form early import intermediates in isolated pea chloroplasts

Paula Row, John C Gray

Journal of Experimental Botany, Volume: 52, Issue: 354, Pages: 47 - 56

Swansea University Author: Paula Row

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DOI (Published version): 10.1093/jexbot/52.354.47

Abstract

In order to ascertain whether there is one site for the import of precursor proteins into chloroplasts or whether different precursor proteins are imported via different import machineries, chloroplasts were incubated with large quantities of the precursor of the 33 kDa subunit of the oxygen-evolvin...

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Published in: Journal of Experimental Botany
Published: 2001
Online Access: http://jxb.oxfordjournals.org/content/52/354/47.full.pdf
URI: https://cronfa.swan.ac.uk/Record/cronfa18375
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fullrecord <?xml version="1.0"?><rfc1807><datestamp>2014-09-10T14:31:44.6805681</datestamp><bib-version>v2</bib-version><id>18375</id><entry>2014-09-10</entry><title>Chloroplast precursor proteins compete to form early import intermediates in isolated pea chloroplasts</title><swanseaauthors><author><sid>99bb528b2f8fb62aabbdad101d53ba96</sid><firstname>Paula</firstname><surname>Row</surname><name>Paula Row</name><active>true</active><ethesisStudent>false</ethesisStudent></author></swanseaauthors><date>2014-09-10</date><deptcode>BMS</deptcode><abstract>In order to ascertain whether there is one site for the import of precursor proteins into chloroplasts or whether different precursor proteins are imported via different import machineries, chloroplasts were incubated with large quantities of the precursor of the 33 kDa subunit of the oxygen-evolving complex (pOE33) or the precursor of the light-harvesting chlorophyll a/b-binding protein (pLHCP) and tested for their ability to import a wide range of other chloroplast precursor proteins. Both pOE33 and pLHCP competed for import into chloroplasts with precursors of the stromally-targeted small subunit of Rubisco (pSSu), ferredoxin NADP(+) reductase (pFNR) and porphobilinogen deaminase; the thylakoid membrane proteins LHCP and the Rieske iron-sulphur protein (pRieske protein); ferrochelatase and the gamma subunit of the ATP synthase (which are both associated with the thylakoid membrane); the thylakoid lumenal protein plastocyanin and the phosphate translocator, an integral membrane protein of the inner envelope. The concentrations of pOE33 or pLHCP required to cause half-maximal inhibition of import ranged between 0.2 and 4.9 microM. These results indicate that all of these proteins are imported into the chloroplast by a common import machinery. Incubation of chloroplasts with pOE33 inhibited the formation of early import intermediates of pSSu, pFNR and pRieske protein.</abstract><type>Journal Article</type><journal>Journal of Experimental Botany</journal><volume>52</volume><journalNumber>354</journalNumber><paginationStart>47</paginationStart><paginationEnd>56</paginationEnd><publisher/><keywords>In order to ascertain whether there is one site for the import of precursor proteins into chloroplasts or whether different precursor proteins are imported via different import machineries, chloroplasts were incubated with large quantities of the precursor of the 33 kDa subunit of the oxygen-evolving complex (pOE33) or the precursor of the light-harvesting chlorophyll a/b-binding protein (pLHCP) and tested for their ability to import a wide range of other chloroplast precursor proteins. Both pOE33 and pLHCP competed for import into chloroplasts with precursors of the stromally-targeted small subunit of Rubisco (pSSu), ferredoxin NADP(+) reductase (pFNR) and porphobilinogen deaminase; the thylakoid membrane proteins LHCP and the Rieske iron-sulphur protein (pRieske protein); ferrochelatase and the gamma subunit of the ATP synthase (which are both associated with the thylakoid membrane); the thylakoid lumenal protein plastocyanin and the phosphate translocator, an integral membrane protein of the inner envelope. The concentrations of pOE33 or pLHCP required to cause half-maximal inhibition of import ranged between 0.2 and 4.9 microM. These results indicate that all of these proteins are imported into the chloroplast by a common import machinery. Incubation of chloroplasts with pOE33 inhibited the formation of early import intermediates of pSSu, pFNR and pRieske protein.</keywords><publishedDay>31</publishedDay><publishedMonth>12</publishedMonth><publishedYear>2001</publishedYear><publishedDate>2001-12-31</publishedDate><doi>10.1093/jexbot/52.354.47</doi><url>http://jxb.oxfordjournals.org/content/52/354/47.full.pdf</url><notes/><college>COLLEGE NANME</college><department>Biomedical Sciences</department><CollegeCode>COLLEGE CODE</CollegeCode><DepartmentCode>BMS</DepartmentCode><institution>Swansea University</institution><apcterm/><lastEdited>2014-09-10T14:31:44.6805681</lastEdited><Created>2014-09-10T13:25:35.5369479</Created><path><level id="1">Faculty of Medicine, Health and Life Sciences</level><level id="2">Swansea University Medical School - Medicine</level></path><authors><author><firstname>Paula</firstname><surname>Row</surname><order>1</order></author><author><firstname>John C</firstname><surname>Gray</surname><order>2</order></author></authors><documents/><OutputDurs/></rfc1807>
spelling 2014-09-10T14:31:44.6805681 v2 18375 2014-09-10 Chloroplast precursor proteins compete to form early import intermediates in isolated pea chloroplasts 99bb528b2f8fb62aabbdad101d53ba96 Paula Row Paula Row true false 2014-09-10 BMS In order to ascertain whether there is one site for the import of precursor proteins into chloroplasts or whether different precursor proteins are imported via different import machineries, chloroplasts were incubated with large quantities of the precursor of the 33 kDa subunit of the oxygen-evolving complex (pOE33) or the precursor of the light-harvesting chlorophyll a/b-binding protein (pLHCP) and tested for their ability to import a wide range of other chloroplast precursor proteins. Both pOE33 and pLHCP competed for import into chloroplasts with precursors of the stromally-targeted small subunit of Rubisco (pSSu), ferredoxin NADP(+) reductase (pFNR) and porphobilinogen deaminase; the thylakoid membrane proteins LHCP and the Rieske iron-sulphur protein (pRieske protein); ferrochelatase and the gamma subunit of the ATP synthase (which are both associated with the thylakoid membrane); the thylakoid lumenal protein plastocyanin and the phosphate translocator, an integral membrane protein of the inner envelope. The concentrations of pOE33 or pLHCP required to cause half-maximal inhibition of import ranged between 0.2 and 4.9 microM. These results indicate that all of these proteins are imported into the chloroplast by a common import machinery. Incubation of chloroplasts with pOE33 inhibited the formation of early import intermediates of pSSu, pFNR and pRieske protein. Journal Article Journal of Experimental Botany 52 354 47 56 In order to ascertain whether there is one site for the import of precursor proteins into chloroplasts or whether different precursor proteins are imported via different import machineries, chloroplasts were incubated with large quantities of the precursor of the 33 kDa subunit of the oxygen-evolving complex (pOE33) or the precursor of the light-harvesting chlorophyll a/b-binding protein (pLHCP) and tested for their ability to import a wide range of other chloroplast precursor proteins. Both pOE33 and pLHCP competed for import into chloroplasts with precursors of the stromally-targeted small subunit of Rubisco (pSSu), ferredoxin NADP(+) reductase (pFNR) and porphobilinogen deaminase; the thylakoid membrane proteins LHCP and the Rieske iron-sulphur protein (pRieske protein); ferrochelatase and the gamma subunit of the ATP synthase (which are both associated with the thylakoid membrane); the thylakoid lumenal protein plastocyanin and the phosphate translocator, an integral membrane protein of the inner envelope. The concentrations of pOE33 or pLHCP required to cause half-maximal inhibition of import ranged between 0.2 and 4.9 microM. These results indicate that all of these proteins are imported into the chloroplast by a common import machinery. Incubation of chloroplasts with pOE33 inhibited the formation of early import intermediates of pSSu, pFNR and pRieske protein. 31 12 2001 2001-12-31 10.1093/jexbot/52.354.47 http://jxb.oxfordjournals.org/content/52/354/47.full.pdf COLLEGE NANME Biomedical Sciences COLLEGE CODE BMS Swansea University 2014-09-10T14:31:44.6805681 2014-09-10T13:25:35.5369479 Faculty of Medicine, Health and Life Sciences Swansea University Medical School - Medicine Paula Row 1 John C Gray 2
title Chloroplast precursor proteins compete to form early import intermediates in isolated pea chloroplasts
spellingShingle Chloroplast precursor proteins compete to form early import intermediates in isolated pea chloroplasts
Paula Row
title_short Chloroplast precursor proteins compete to form early import intermediates in isolated pea chloroplasts
title_full Chloroplast precursor proteins compete to form early import intermediates in isolated pea chloroplasts
title_fullStr Chloroplast precursor proteins compete to form early import intermediates in isolated pea chloroplasts
title_full_unstemmed Chloroplast precursor proteins compete to form early import intermediates in isolated pea chloroplasts
title_sort Chloroplast precursor proteins compete to form early import intermediates in isolated pea chloroplasts
author_id_str_mv 99bb528b2f8fb62aabbdad101d53ba96
author_id_fullname_str_mv 99bb528b2f8fb62aabbdad101d53ba96_***_Paula Row
author Paula Row
author2 Paula Row
John C Gray
format Journal article
container_title Journal of Experimental Botany
container_volume 52
container_issue 354
container_start_page 47
publishDate 2001
institution Swansea University
doi_str_mv 10.1093/jexbot/52.354.47
college_str Faculty of Medicine, Health and Life Sciences
hierarchytype
hierarchy_top_id facultyofmedicinehealthandlifesciences
hierarchy_top_title Faculty of Medicine, Health and Life Sciences
hierarchy_parent_id facultyofmedicinehealthandlifesciences
hierarchy_parent_title Faculty of Medicine, Health and Life Sciences
department_str Swansea University Medical School - Medicine{{{_:::_}}}Faculty of Medicine, Health and Life Sciences{{{_:::_}}}Swansea University Medical School - Medicine
url http://jxb.oxfordjournals.org/content/52/354/47.full.pdf
document_store_str 0
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description In order to ascertain whether there is one site for the import of precursor proteins into chloroplasts or whether different precursor proteins are imported via different import machineries, chloroplasts were incubated with large quantities of the precursor of the 33 kDa subunit of the oxygen-evolving complex (pOE33) or the precursor of the light-harvesting chlorophyll a/b-binding protein (pLHCP) and tested for their ability to import a wide range of other chloroplast precursor proteins. Both pOE33 and pLHCP competed for import into chloroplasts with precursors of the stromally-targeted small subunit of Rubisco (pSSu), ferredoxin NADP(+) reductase (pFNR) and porphobilinogen deaminase; the thylakoid membrane proteins LHCP and the Rieske iron-sulphur protein (pRieske protein); ferrochelatase and the gamma subunit of the ATP synthase (which are both associated with the thylakoid membrane); the thylakoid lumenal protein plastocyanin and the phosphate translocator, an integral membrane protein of the inner envelope. The concentrations of pOE33 or pLHCP required to cause half-maximal inhibition of import ranged between 0.2 and 4.9 microM. These results indicate that all of these proteins are imported into the chloroplast by a common import machinery. Incubation of chloroplasts with pOE33 inhibited the formation of early import intermediates of pSSu, pFNR and pRieske protein.
published_date 2001-12-31T03:21:32Z
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score 11.03559

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