Starch synthase 4 is located in the thylakoid membrane and interacts with plastoglobule‐associated proteins in Arabidopsis
Starch synthesis requires the formation of a primer that can be subsequently elongated and branched. How this primer is produced, however, remains unknown. The control of the number of starch granules produced per chloroplast is also a matter of debate. We previously showed starch synthase 4 (SS4) t...
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| Veröffentlicht in: | The Plant journal : for cell and molecular biology 2014-10, Vol.80 (2), p.305-316 |
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| creator | Gámez‐Arjona, Francisco M Raynaud, Sandy Ragel, Paula Mérida, Ángel |
| description | Starch synthesis requires the formation of a primer that can be subsequently elongated and branched. How this primer is produced, however, remains unknown. The control of the number of starch granules produced per chloroplast is also a matter of debate. We previously showed starch synthase 4 (SS4) to be involved in both processes, although the mechanisms involved are yet to be fully characterised. The present work shows that SS4 displays a specific localization different from other starch synthases. Thus, this protein is located in specific areas of the thylakoid membrane and interacts with the proteins fibrillin 1a (FBN1a) and 1b (FBN1b), which are mainly located in plastoglobules. SS4 would seem to be associated with plastoglobules attached to the thylakoids (or to that portion of the thylakoids where plastoglobules have originated), forming a complex that includes the FBN1s and other as‐yet unidentified proteins. The present results also indicate that the localization pattern of SS4, and its interactions with the FBN1 proteins, are mediated through its N‐terminal region, which contains two long coiled‐coil motifs. The localization of SS4 in specific areas of the thylakoid membrane suggests that starch granules are originated at specific regions of the chloroplast. |
| doi_str_mv | 10.1111/tpj.12633 |
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How this primer is produced, however, remains unknown. The control of the number of starch granules produced per chloroplast is also a matter of debate. We previously showed starch synthase 4 (SS4) to be involved in both processes, although the mechanisms involved are yet to be fully characterised. The present work shows that SS4 displays a specific localization different from other starch synthases. Thus, this protein is located in specific areas of the thylakoid membrane and interacts with the proteins fibrillin 1a (FBN1a) and 1b (FBN1b), which are mainly located in plastoglobules. SS4 would seem to be associated with plastoglobules attached to the thylakoids (or to that portion of the thylakoids where plastoglobules have originated), forming a complex that includes the FBN1s and other as‐yet unidentified proteins. The present results also indicate that the localization pattern of SS4, and its interactions with the FBN1 proteins, are mediated through its N‐terminal region, which contains two long coiled‐coil motifs. The localization of SS4 in specific areas of the thylakoid membrane suggests that starch granules are originated at specific regions of the chloroplast.</description><identifier>ISSN: 0960-7412</identifier><identifier>EISSN: 1365-313X</identifier><identifier>DOI: 10.1111/tpj.12633</identifier><identifier>PMID: 25088399</identifier><language>eng</language><publisher>England: Blackwell Scientific Publishers and BIOS Scientific Publishers in association with the Society for Experimental Biology</publisher><subject>Arabidopsis ; Arabidopsis - enzymology ; Arabidopsis Proteins - metabolism ; Arabidopsis thaliana ; Botany ; Carbohydrates ; Chloroplasts - enzymology ; Enzymes ; fibrillins ; Photosynthesis ; plastoglobules ; Protein Binding ; Proteins ; protein–protein interaction ; starch granules ; starch synthase ; Starch Synthase - metabolism ; thylakoids ; Thylakoids - enzymology ; Two-Hybrid System Techniques</subject><ispartof>The Plant journal : for cell and molecular biology, 2014-10, Vol.80 (2), p.305-316</ispartof><rights>2014 The Authors The Plant Journal © 2014 John Wiley & Sons Ltd</rights><rights>2014 The Authors The Plant Journal © 2014 John Wiley & Sons Ltd.</rights><rights>Copyright © 2014 John Wiley & Sons Ltd and the Society for Experimental Biology</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4453-a54a4704d047f9a2eb19ca44d2779a4c06eb0bf672777d2cf9aa1e4dda16969b3</citedby><cites>FETCH-LOGICAL-c4453-a54a4704d047f9a2eb19ca44d2779a4c06eb0bf672777d2cf9aa1e4dda16969b3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1111%2Ftpj.12633$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Ftpj.12633$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,1427,27901,27902,45550,45551,46384,46808</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/25088399$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Gámez‐Arjona, Francisco M</creatorcontrib><creatorcontrib>Raynaud, Sandy</creatorcontrib><creatorcontrib>Ragel, Paula</creatorcontrib><creatorcontrib>Mérida, Ángel</creatorcontrib><title>Starch synthase 4 is located in the thylakoid membrane and interacts with plastoglobule‐associated proteins in Arabidopsis</title><title>The Plant journal : for cell and molecular biology</title><addtitle>Plant J</addtitle><description>Starch synthesis requires the formation of a primer that can be subsequently elongated and branched. How this primer is produced, however, remains unknown. The control of the number of starch granules produced per chloroplast is also a matter of debate. We previously showed starch synthase 4 (SS4) to be involved in both processes, although the mechanisms involved are yet to be fully characterised. The present work shows that SS4 displays a specific localization different from other starch synthases. Thus, this protein is located in specific areas of the thylakoid membrane and interacts with the proteins fibrillin 1a (FBN1a) and 1b (FBN1b), which are mainly located in plastoglobules. SS4 would seem to be associated with plastoglobules attached to the thylakoids (or to that portion of the thylakoids where plastoglobules have originated), forming a complex that includes the FBN1s and other as‐yet unidentified proteins. The present results also indicate that the localization pattern of SS4, and its interactions with the FBN1 proteins, are mediated through its N‐terminal region, which contains two long coiled‐coil motifs. The localization of SS4 in specific areas of the thylakoid membrane suggests that starch granules are originated at specific regions of the chloroplast.</description><subject>Arabidopsis</subject><subject>Arabidopsis - enzymology</subject><subject>Arabidopsis Proteins - metabolism</subject><subject>Arabidopsis thaliana</subject><subject>Botany</subject><subject>Carbohydrates</subject><subject>Chloroplasts - enzymology</subject><subject>Enzymes</subject><subject>fibrillins</subject><subject>Photosynthesis</subject><subject>plastoglobules</subject><subject>Protein Binding</subject><subject>Proteins</subject><subject>protein–protein interaction</subject><subject>starch granules</subject><subject>starch synthase</subject><subject>Starch Synthase - metabolism</subject><subject>thylakoids</subject><subject>Thylakoids - enzymology</subject><subject>Two-Hybrid System Techniques</subject><issn>0960-7412</issn><issn>1365-313X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2014</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc9qFTEUh4Mo9lpd-AIacKOLaZNJJpksS_EvBYW24C6cSTK9uc5MpkmGcsGFj-Az-iTm9rYuBDEQwuF8-TiHH0LPKTmi5RzneXNEa8HYA7SiTDQVo-zrQ7QiSpBKclofoCcpbQihkgn-GB3UDWlbptQKfT_PEM0ap-2U15Ac5tgnPAQD2VnsJ5zXrtztAN-Ct3h0YxdhchimXTe7CCYnfOPzGs8DpByuhtAtg_v14yekFIy_9cwxZOentBOeROi8DXPy6Sl61MOQ3LO79xBdvnt7cfqhOvv8_uPpyVllOG9YBQ0HLgm3hMteQe06qgxwbmspFXBDhOtI1wtZamlrUxigjlsLVCihOnaIXu-9ZY7rxaWsR5-MG4aySViSpq2irVANZ_9Hm1YQJSXjBX31F7oJS5zKIoUSQpSRlSrUmz1lYkgpul7P0Y8Qt5oSvUtPl_T0bXqFfXFnXLrR2T_kfVwFON4DN35w23-b9MWXT_fKl_sfPQQNV9EnfXleE9oQQmoiWMt-AwrHryk</recordid><startdate>201410</startdate><enddate>201410</enddate><creator>Gámez‐Arjona, Francisco M</creator><creator>Raynaud, Sandy</creator><creator>Ragel, Paula</creator><creator>Mérida, Ángel</creator><general>Blackwell Scientific Publishers and BIOS Scientific Publishers in association with the Society for Experimental Biology</general><general>Blackwell Publishing Ltd</general><scope>FBQ</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>7QO</scope><scope>7QP</scope><scope>7QR</scope><scope>7TM</scope><scope>8FD</scope><scope>FR3</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>201410</creationdate><title>Starch synthase 4 is located in the thylakoid membrane and interacts with plastoglobule‐associated proteins in Arabidopsis</title><author>Gámez‐Arjona, Francisco M ; Raynaud, Sandy ; Ragel, Paula ; Mérida, Ángel</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4453-a54a4704d047f9a2eb19ca44d2779a4c06eb0bf672777d2cf9aa1e4dda16969b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2014</creationdate><topic>Arabidopsis</topic><topic>Arabidopsis - enzymology</topic><topic>Arabidopsis Proteins - metabolism</topic><topic>Arabidopsis thaliana</topic><topic>Botany</topic><topic>Carbohydrates</topic><topic>Chloroplasts - enzymology</topic><topic>Enzymes</topic><topic>fibrillins</topic><topic>Photosynthesis</topic><topic>plastoglobules</topic><topic>Protein Binding</topic><topic>Proteins</topic><topic>protein–protein interaction</topic><topic>starch granules</topic><topic>starch synthase</topic><topic>Starch Synthase - metabolism</topic><topic>thylakoids</topic><topic>Thylakoids - enzymology</topic><topic>Two-Hybrid System Techniques</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Gámez‐Arjona, Francisco M</creatorcontrib><creatorcontrib>Raynaud, Sandy</creatorcontrib><creatorcontrib>Ragel, Paula</creatorcontrib><creatorcontrib>Mérida, Ángel</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Biotechnology Research Abstracts</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>The Plant journal : for cell and molecular biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Gámez‐Arjona, Francisco M</au><au>Raynaud, Sandy</au><au>Ragel, Paula</au><au>Mérida, Ángel</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Starch synthase 4 is located in the thylakoid membrane and interacts with plastoglobule‐associated proteins in Arabidopsis</atitle><jtitle>The Plant journal : for cell and molecular biology</jtitle><addtitle>Plant J</addtitle><date>2014-10</date><risdate>2014</risdate><volume>80</volume><issue>2</issue><spage>305</spage><epage>316</epage><pages>305-316</pages><issn>0960-7412</issn><eissn>1365-313X</eissn><abstract>Starch synthesis requires the formation of a primer that can be subsequently elongated and branched. How this primer is produced, however, remains unknown. The control of the number of starch granules produced per chloroplast is also a matter of debate. We previously showed starch synthase 4 (SS4) to be involved in both processes, although the mechanisms involved are yet to be fully characterised. The present work shows that SS4 displays a specific localization different from other starch synthases. Thus, this protein is located in specific areas of the thylakoid membrane and interacts with the proteins fibrillin 1a (FBN1a) and 1b (FBN1b), which are mainly located in plastoglobules. SS4 would seem to be associated with plastoglobules attached to the thylakoids (or to that portion of the thylakoids where plastoglobules have originated), forming a complex that includes the FBN1s and other as‐yet unidentified proteins. The present results also indicate that the localization pattern of SS4, and its interactions with the FBN1 proteins, are mediated through its N‐terminal region, which contains two long coiled‐coil motifs. The localization of SS4 in specific areas of the thylakoid membrane suggests that starch granules are originated at specific regions of the chloroplast.</abstract><cop>England</cop><pub>Blackwell Scientific Publishers and BIOS Scientific Publishers in association with the Society for Experimental Biology</pub><pmid>25088399</pmid><doi>10.1111/tpj.12633</doi><tpages>12</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Arabidopsis Arabidopsis - enzymology Arabidopsis Proteins - metabolism Arabidopsis thaliana Botany Carbohydrates Chloroplasts - enzymology Enzymes fibrillins Photosynthesis plastoglobules Protein Binding Proteins protein–protein interaction starch granules starch synthase Starch Synthase - metabolism thylakoids Thylakoids - enzymology Two-Hybrid System Techniques |
| title | Starch synthase 4 is located in the thylakoid membrane and interacts with plastoglobule‐associated proteins in Arabidopsis |
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