Impact of C‐terminal truncations in the Arabidopsis Rab escort protein (REP) on REP–Rab interaction and plant fertility
SUMMARY Lipid anchors are common post‐translational modifications for proteins engaged in signaling and vesicular transport in eukaryotic cells. Rab proteins are geranylgeranylated at their C‐termini, a modification which is important for their stable binding to lipid bilayers. The Rab escort protei...
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| Veröffentlicht in: | The Plant journal : for cell and molecular biology 2021-12, Vol.108 (5), p.1400-1421 |
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| creator | Gutkowska, Małgorzata Kaus‐Drobek, Magdalena Hoffman‐Sommer, Marta Małgorzata Pamuła, Magdalena Daria Leja, Anna Perycz, Małgorzata Lichocka, Małgorzata Witek, Agnieszka Wojtas, Magdalena Dadlez, Michał Swiezewska, Ewa Surmacz, Liliana |
| description | SUMMARY
Lipid anchors are common post‐translational modifications for proteins engaged in signaling and vesicular transport in eukaryotic cells. Rab proteins are geranylgeranylated at their C‐termini, a modification which is important for their stable binding to lipid bilayers. The Rab escort protein (REP) is an accessory protein of the Rab geranylgeranyl transferase (RGT) complex and it is obligatory for Rab prenylation. While REP–Rab interactions have been studied by biochemical, structural, and genetic methods in animals and yeast, data on the plant RGT complex are still limited. Here we use hydrogen–deuterium exchange mass spectrometry (HDX‐MS) to describe the structural basis of plant REP–Rab binding. The obtained results show that the interaction of REP with Rabs is highly dynamic and involves specific structural changes in both partners. In some cases the Rab and REP regions involved in the interaction are molecule‐specific, and in other cases they are common for a subset of Rabs. In particular, the C‐terminus of REP is not involved in binding of unprenylated Rab proteins in plants, in contrast to mammalian REP. In line with this, a C‐terminal REP truncation does not have pronounced phenotypic effects in planta. On the contrary, a complete lack of functional REP leads to male sterility in Arabidopsis: pollen grains develop in the anthers, but they do not germinate efficiently and hence are unable to transmit the mutated allele. The presented data show that the mechanism of action of REP in the process of Rab geranylgeranylation is different in plants than in animals or yeast.
Significance Statement
The Rab escort protein (REP) is part of the Rab geranylgeranyl transferase (RGT) complex and it is obligatory for Rab prenylation. We show by biochemical, biophysical, and genetic methods that the mechanism of action of REP, in particular the role of its C‐terminus in Rab binding and prenylation, is different in plants than in animals or yeast. |
| doi_str_mv | 10.1111/tpj.15519 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_9293207</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>2603915224</sourcerecordid><originalsourceid>FETCH-LOGICAL-c4439-b5508a33141dbfd7744493379a4dab2d9dfe40ae656c9662d01f930335fc90503</originalsourceid><addsrcrecordid>eNp1kc9qFTEUh4Mo9tq68AUk4KZdTJv_02yEcqm2UrCUFtyFTJKxucwkY5JRLm76CIJv2Cdp6q1FBc_mLM7HxznnB8ArjPZxrYMyrfYx51g-AQtMBW8opp-eggWSAjUtw2QLvMh5hRBuqWDPwRZlXBJE2AJ8Px0nbQqMPVze3vwoLo0-6AGWNAeji48hQx9guXbwKOnO2zhln-GF7qDLJqYCpxSLq8juxfH5HowB1n578_Oe8KH6qr1aoA4WToMOBfYuFT_4st4Bz3o9ZPfyoW-Dq3fHl8uT5uzj-9Pl0VljGKOy6ThHh5pSzLDtetu2jDFJaSs1s7ojVtreMaSd4MJIIYhFuJcUUcp7IxFHdBu83XinuRudNS6UpAc1JT_qtFZRe_X3JPhr9Tl-VZJISlBbBbsPghS_zC4XNfps3FDPcXHOivD2sBWcYl7RN_-gqzin-tFKCUQl5oSwSu1tKJNizsn1j8tgpO4jVTVS9SvSyr7-c_tH8neGFTjYAN_84Nb_N6nL8w8b5R1J_K1a</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2603915224</pqid></control><display><type>article</type><title>Impact of C‐terminal truncations in the Arabidopsis Rab escort protein (REP) on REP–Rab interaction and plant fertility</title><source>MEDLINE</source><source>Wiley Online Library Free Content</source><source>IngentaConnect Free/Open Access Journals</source><source>EZB-FREE-00999 freely available EZB journals</source><source>Wiley Online Library All Journals</source><creator>Gutkowska, Małgorzata ; Kaus‐Drobek, Magdalena ; Hoffman‐Sommer, Marta ; Małgorzata Pamuła, Magdalena ; Daria Leja, Anna ; Perycz, Małgorzata ; Lichocka, Małgorzata ; Witek, Agnieszka ; Wojtas, Magdalena ; Dadlez, Michał ; Swiezewska, Ewa ; Surmacz, Liliana</creator><creatorcontrib>Gutkowska, Małgorzata ; Kaus‐Drobek, Magdalena ; Hoffman‐Sommer, Marta ; Małgorzata Pamuła, Magdalena ; Daria Leja, Anna ; Perycz, Małgorzata ; Lichocka, Małgorzata ; Witek, Agnieszka ; Wojtas, Magdalena ; Dadlez, Michał ; Swiezewska, Ewa ; Surmacz, Liliana</creatorcontrib><description>SUMMARY
Lipid anchors are common post‐translational modifications for proteins engaged in signaling and vesicular transport in eukaryotic cells. Rab proteins are geranylgeranylated at their C‐termini, a modification which is important for their stable binding to lipid bilayers. The Rab escort protein (REP) is an accessory protein of the Rab geranylgeranyl transferase (RGT) complex and it is obligatory for Rab prenylation. While REP–Rab interactions have been studied by biochemical, structural, and genetic methods in animals and yeast, data on the plant RGT complex are still limited. Here we use hydrogen–deuterium exchange mass spectrometry (HDX‐MS) to describe the structural basis of plant REP–Rab binding. The obtained results show that the interaction of REP with Rabs is highly dynamic and involves specific structural changes in both partners. In some cases the Rab and REP regions involved in the interaction are molecule‐specific, and in other cases they are common for a subset of Rabs. In particular, the C‐terminus of REP is not involved in binding of unprenylated Rab proteins in plants, in contrast to mammalian REP. In line with this, a C‐terminal REP truncation does not have pronounced phenotypic effects in planta. On the contrary, a complete lack of functional REP leads to male sterility in Arabidopsis: pollen grains develop in the anthers, but they do not germinate efficiently and hence are unable to transmit the mutated allele. The presented data show that the mechanism of action of REP in the process of Rab geranylgeranylation is different in plants than in animals or yeast.
Significance Statement
The Rab escort protein (REP) is part of the Rab geranylgeranyl transferase (RGT) complex and it is obligatory for Rab prenylation. We show by biochemical, biophysical, and genetic methods that the mechanism of action of REP, in particular the role of its C‐terminus in Rab binding and prenylation, is different in plants than in animals or yeast.</description><identifier>ISSN: 0960-7412</identifier><identifier>EISSN: 1365-313X</identifier><identifier>DOI: 10.1111/tpj.15519</identifier><identifier>PMID: 34592024</identifier><language>eng</language><publisher>England: Blackwell Publishing Ltd</publisher><subject>Adaptor Proteins, Signal Transducing - genetics ; Adaptor Proteins, Signal Transducing - metabolism ; Alkyl and Aryl Transferases - genetics ; Alkyl and Aryl Transferases - metabolism ; Animals ; Anthers ; Arabidopsis ; Arabidopsis - genetics ; Arabidopsis - metabolism ; Arabidopsis Proteins - genetics ; Arabidopsis Proteins - metabolism ; Arabidopsis thaliana ; Binding ; Deuterium ; Fertility ; Geranylgeranyltransferase ; HDX‐MS ; Hydrogen-deuterium exchange ; Lipid bilayers ; Lipids ; Male sterility ; Mass spectrometry ; Mass spectroscopy ; Original ; Plant Infertility ; Pollen ; Protein Binding ; protein geranylgeranylation ; Protein Prenylation ; Protein Processing, Post-Translational ; Proteins ; Rab escort protein ; rab GTP-Binding Proteins - genetics ; rab GTP-Binding Proteins - metabolism ; Rab proteins ; Yeast ; Yeasts</subject><ispartof>The Plant journal : for cell and molecular biology, 2021-12, Vol.108 (5), p.1400-1421</ispartof><rights>2021 The Authors. published by Society for Experimental Biology and John Wiley & Sons Ltd.</rights><rights>2021 The Authors. The Plant Journal published by Society for Experimental Biology and John Wiley & Sons Ltd.</rights><rights>2021. This article is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4439-b5508a33141dbfd7744493379a4dab2d9dfe40ae656c9662d01f930335fc90503</citedby><cites>FETCH-LOGICAL-c4439-b5508a33141dbfd7744493379a4dab2d9dfe40ae656c9662d01f930335fc90503</cites><orcidid>0000-0002-1451-5967 ; 0000-0002-9517-1608 ; 0000-0001-8811-5176 ; 0000-0002-3439-8948 ; 0000-0001-6584-7964 ; 0000-0001-6202-4567 ; 0000-0003-3154-6594 ; 0000-0002-9894-8195</orcidid></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.15519$$EPDF$$P50$$Gwiley$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Ftpj.15519$$EHTML$$P50$$Gwiley$$Hfree_for_read</linktohtml><link.rule.ids>230,314,780,784,885,1416,1432,27922,27923,45572,45573,46407,46831</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/34592024$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Gutkowska, Małgorzata</creatorcontrib><creatorcontrib>Kaus‐Drobek, Magdalena</creatorcontrib><creatorcontrib>Hoffman‐Sommer, Marta</creatorcontrib><creatorcontrib>Małgorzata Pamuła, Magdalena</creatorcontrib><creatorcontrib>Daria Leja, Anna</creatorcontrib><creatorcontrib>Perycz, Małgorzata</creatorcontrib><creatorcontrib>Lichocka, Małgorzata</creatorcontrib><creatorcontrib>Witek, Agnieszka</creatorcontrib><creatorcontrib>Wojtas, Magdalena</creatorcontrib><creatorcontrib>Dadlez, Michał</creatorcontrib><creatorcontrib>Swiezewska, Ewa</creatorcontrib><creatorcontrib>Surmacz, Liliana</creatorcontrib><title>Impact of C‐terminal truncations in the Arabidopsis Rab escort protein (REP) on REP–Rab interaction and plant fertility</title><title>The Plant journal : for cell and molecular biology</title><addtitle>Plant J</addtitle><description>SUMMARY
Lipid anchors are common post‐translational modifications for proteins engaged in signaling and vesicular transport in eukaryotic cells. Rab proteins are geranylgeranylated at their C‐termini, a modification which is important for their stable binding to lipid bilayers. The Rab escort protein (REP) is an accessory protein of the Rab geranylgeranyl transferase (RGT) complex and it is obligatory for Rab prenylation. While REP–Rab interactions have been studied by biochemical, structural, and genetic methods in animals and yeast, data on the plant RGT complex are still limited. Here we use hydrogen–deuterium exchange mass spectrometry (HDX‐MS) to describe the structural basis of plant REP–Rab binding. The obtained results show that the interaction of REP with Rabs is highly dynamic and involves specific structural changes in both partners. In some cases the Rab and REP regions involved in the interaction are molecule‐specific, and in other cases they are common for a subset of Rabs. In particular, the C‐terminus of REP is not involved in binding of unprenylated Rab proteins in plants, in contrast to mammalian REP. In line with this, a C‐terminal REP truncation does not have pronounced phenotypic effects in planta. On the contrary, a complete lack of functional REP leads to male sterility in Arabidopsis: pollen grains develop in the anthers, but they do not germinate efficiently and hence are unable to transmit the mutated allele. The presented data show that the mechanism of action of REP in the process of Rab geranylgeranylation is different in plants than in animals or yeast.
Significance Statement
The Rab escort protein (REP) is part of the Rab geranylgeranyl transferase (RGT) complex and it is obligatory for Rab prenylation. We show by biochemical, biophysical, and genetic methods that the mechanism of action of REP, in particular the role of its C‐terminus in Rab binding and prenylation, is different in plants than in animals or yeast.</description><subject>Adaptor Proteins, Signal Transducing - genetics</subject><subject>Adaptor Proteins, Signal Transducing - metabolism</subject><subject>Alkyl and Aryl Transferases - genetics</subject><subject>Alkyl and Aryl Transferases - metabolism</subject><subject>Animals</subject><subject>Anthers</subject><subject>Arabidopsis</subject><subject>Arabidopsis - genetics</subject><subject>Arabidopsis - metabolism</subject><subject>Arabidopsis Proteins - genetics</subject><subject>Arabidopsis Proteins - metabolism</subject><subject>Arabidopsis thaliana</subject><subject>Binding</subject><subject>Deuterium</subject><subject>Fertility</subject><subject>Geranylgeranyltransferase</subject><subject>HDX‐MS</subject><subject>Hydrogen-deuterium exchange</subject><subject>Lipid bilayers</subject><subject>Lipids</subject><subject>Male sterility</subject><subject>Mass spectrometry</subject><subject>Mass spectroscopy</subject><subject>Original</subject><subject>Plant Infertility</subject><subject>Pollen</subject><subject>Protein Binding</subject><subject>protein geranylgeranylation</subject><subject>Protein Prenylation</subject><subject>Protein Processing, Post-Translational</subject><subject>Proteins</subject><subject>Rab escort protein</subject><subject>rab GTP-Binding Proteins - genetics</subject><subject>rab GTP-Binding Proteins - metabolism</subject><subject>Rab proteins</subject><subject>Yeast</subject><subject>Yeasts</subject><issn>0960-7412</issn><issn>1365-313X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2021</creationdate><recordtype>article</recordtype><sourceid>24P</sourceid><sourceid>WIN</sourceid><sourceid>EIF</sourceid><recordid>eNp1kc9qFTEUh4Mo9tq68AUk4KZdTJv_02yEcqm2UrCUFtyFTJKxucwkY5JRLm76CIJv2Cdp6q1FBc_mLM7HxznnB8ArjPZxrYMyrfYx51g-AQtMBW8opp-eggWSAjUtw2QLvMh5hRBuqWDPwRZlXBJE2AJ8Px0nbQqMPVze3vwoLo0-6AGWNAeji48hQx9guXbwKOnO2zhln-GF7qDLJqYCpxSLq8juxfH5HowB1n578_Oe8KH6qr1aoA4WToMOBfYuFT_4st4Bz3o9ZPfyoW-Dq3fHl8uT5uzj-9Pl0VljGKOy6ThHh5pSzLDtetu2jDFJaSs1s7ojVtreMaSd4MJIIYhFuJcUUcp7IxFHdBu83XinuRudNS6UpAc1JT_qtFZRe_X3JPhr9Tl-VZJISlBbBbsPghS_zC4XNfps3FDPcXHOivD2sBWcYl7RN_-gqzin-tFKCUQl5oSwSu1tKJNizsn1j8tgpO4jVTVS9SvSyr7-c_tH8neGFTjYAN_84Nb_N6nL8w8b5R1J_K1a</recordid><startdate>202112</startdate><enddate>202112</enddate><creator>Gutkowska, Małgorzata</creator><creator>Kaus‐Drobek, Magdalena</creator><creator>Hoffman‐Sommer, Marta</creator><creator>Małgorzata Pamuła, Magdalena</creator><creator>Daria Leja, Anna</creator><creator>Perycz, Małgorzata</creator><creator>Lichocka, Małgorzata</creator><creator>Witek, Agnieszka</creator><creator>Wojtas, Magdalena</creator><creator>Dadlez, Michał</creator><creator>Swiezewska, Ewa</creator><creator>Surmacz, Liliana</creator><general>Blackwell Publishing Ltd</general><general>John Wiley and Sons Inc</general><scope>24P</scope><scope>WIN</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><scope>5PM</scope><orcidid>https://orcid.org/0000-0002-1451-5967</orcidid><orcidid>https://orcid.org/0000-0002-9517-1608</orcidid><orcidid>https://orcid.org/0000-0001-8811-5176</orcidid><orcidid>https://orcid.org/0000-0002-3439-8948</orcidid><orcidid>https://orcid.org/0000-0001-6584-7964</orcidid><orcidid>https://orcid.org/0000-0001-6202-4567</orcidid><orcidid>https://orcid.org/0000-0003-3154-6594</orcidid><orcidid>https://orcid.org/0000-0002-9894-8195</orcidid></search><sort><creationdate>202112</creationdate><title>Impact of C‐terminal truncations in the Arabidopsis Rab escort protein (REP) on REP–Rab interaction and plant fertility</title><author>Gutkowska, Małgorzata ; Kaus‐Drobek, Magdalena ; Hoffman‐Sommer, Marta ; Małgorzata Pamuła, Magdalena ; Daria Leja, Anna ; Perycz, Małgorzata ; Lichocka, Małgorzata ; Witek, Agnieszka ; Wojtas, Magdalena ; Dadlez, Michał ; Swiezewska, Ewa ; Surmacz, Liliana</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4439-b5508a33141dbfd7744493379a4dab2d9dfe40ae656c9662d01f930335fc90503</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2021</creationdate><topic>Adaptor Proteins, Signal Transducing - genetics</topic><topic>Adaptor Proteins, Signal Transducing - metabolism</topic><topic>Alkyl and Aryl Transferases - genetics</topic><topic>Alkyl and Aryl Transferases - metabolism</topic><topic>Animals</topic><topic>Anthers</topic><topic>Arabidopsis</topic><topic>Arabidopsis - genetics</topic><topic>Arabidopsis - metabolism</topic><topic>Arabidopsis Proteins - genetics</topic><topic>Arabidopsis Proteins - metabolism</topic><topic>Arabidopsis thaliana</topic><topic>Binding</topic><topic>Deuterium</topic><topic>Fertility</topic><topic>Geranylgeranyltransferase</topic><topic>HDX‐MS</topic><topic>Hydrogen-deuterium exchange</topic><topic>Lipid bilayers</topic><topic>Lipids</topic><topic>Male sterility</topic><topic>Mass spectrometry</topic><topic>Mass spectroscopy</topic><topic>Original</topic><topic>Plant Infertility</topic><topic>Pollen</topic><topic>Protein Binding</topic><topic>protein geranylgeranylation</topic><topic>Protein Prenylation</topic><topic>Protein Processing, Post-Translational</topic><topic>Proteins</topic><topic>Rab escort protein</topic><topic>rab GTP-Binding Proteins - genetics</topic><topic>rab GTP-Binding Proteins - metabolism</topic><topic>Rab proteins</topic><topic>Yeast</topic><topic>Yeasts</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Gutkowska, Małgorzata</creatorcontrib><creatorcontrib>Kaus‐Drobek, Magdalena</creatorcontrib><creatorcontrib>Hoffman‐Sommer, Marta</creatorcontrib><creatorcontrib>Małgorzata Pamuła, Magdalena</creatorcontrib><creatorcontrib>Daria Leja, Anna</creatorcontrib><creatorcontrib>Perycz, Małgorzata</creatorcontrib><creatorcontrib>Lichocka, Małgorzata</creatorcontrib><creatorcontrib>Witek, Agnieszka</creatorcontrib><creatorcontrib>Wojtas, Magdalena</creatorcontrib><creatorcontrib>Dadlez, Michał</creatorcontrib><creatorcontrib>Swiezewska, Ewa</creatorcontrib><creatorcontrib>Surmacz, Liliana</creatorcontrib><collection>Wiley-Blackwell Open Access Titles</collection><collection>Wiley Online Library Free Content</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><collection>PubMed Central (Full Participant titles)</collection><jtitle>The Plant journal : for cell and molecular biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Gutkowska, Małgorzata</au><au>Kaus‐Drobek, Magdalena</au><au>Hoffman‐Sommer, Marta</au><au>Małgorzata Pamuła, Magdalena</au><au>Daria Leja, Anna</au><au>Perycz, Małgorzata</au><au>Lichocka, Małgorzata</au><au>Witek, Agnieszka</au><au>Wojtas, Magdalena</au><au>Dadlez, Michał</au><au>Swiezewska, Ewa</au><au>Surmacz, Liliana</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Impact of C‐terminal truncations in the Arabidopsis Rab escort protein (REP) on REP–Rab interaction and plant fertility</atitle><jtitle>The Plant journal : for cell and molecular biology</jtitle><addtitle>Plant J</addtitle><date>2021-12</date><risdate>2021</risdate><volume>108</volume><issue>5</issue><spage>1400</spage><epage>1421</epage><pages>1400-1421</pages><issn>0960-7412</issn><eissn>1365-313X</eissn><abstract>SUMMARY
Lipid anchors are common post‐translational modifications for proteins engaged in signaling and vesicular transport in eukaryotic cells. Rab proteins are geranylgeranylated at their C‐termini, a modification which is important for their stable binding to lipid bilayers. The Rab escort protein (REP) is an accessory protein of the Rab geranylgeranyl transferase (RGT) complex and it is obligatory for Rab prenylation. While REP–Rab interactions have been studied by biochemical, structural, and genetic methods in animals and yeast, data on the plant RGT complex are still limited. Here we use hydrogen–deuterium exchange mass spectrometry (HDX‐MS) to describe the structural basis of plant REP–Rab binding. The obtained results show that the interaction of REP with Rabs is highly dynamic and involves specific structural changes in both partners. In some cases the Rab and REP regions involved in the interaction are molecule‐specific, and in other cases they are common for a subset of Rabs. In particular, the C‐terminus of REP is not involved in binding of unprenylated Rab proteins in plants, in contrast to mammalian REP. In line with this, a C‐terminal REP truncation does not have pronounced phenotypic effects in planta. On the contrary, a complete lack of functional REP leads to male sterility in Arabidopsis: pollen grains develop in the anthers, but they do not germinate efficiently and hence are unable to transmit the mutated allele. The presented data show that the mechanism of action of REP in the process of Rab geranylgeranylation is different in plants than in animals or yeast.
Significance Statement
The Rab escort protein (REP) is part of the Rab geranylgeranyl transferase (RGT) complex and it is obligatory for Rab prenylation. We show by biochemical, biophysical, and genetic methods that the mechanism of action of REP, in particular the role of its C‐terminus in Rab binding and prenylation, is different in plants than in animals or yeast.</abstract><cop>England</cop><pub>Blackwell Publishing Ltd</pub><pmid>34592024</pmid><doi>10.1111/tpj.15519</doi><tpages>22</tpages><orcidid>https://orcid.org/0000-0002-1451-5967</orcidid><orcidid>https://orcid.org/0000-0002-9517-1608</orcidid><orcidid>https://orcid.org/0000-0001-8811-5176</orcidid><orcidid>https://orcid.org/0000-0002-3439-8948</orcidid><orcidid>https://orcid.org/0000-0001-6584-7964</orcidid><orcidid>https://orcid.org/0000-0001-6202-4567</orcidid><orcidid>https://orcid.org/0000-0003-3154-6594</orcidid><orcidid>https://orcid.org/0000-0002-9894-8195</orcidid><oa>free_for_read</oa></addata></record> |
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| identifier | ISSN: 0960-7412 |
| ispartof | The Plant journal : for cell and molecular biology, 2021-12, Vol.108 (5), p.1400-1421 |
| issn | 0960-7412 1365-313X |
| language | eng |
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| source | MEDLINE; Wiley Online Library Free Content; IngentaConnect Free/Open Access Journals; EZB-FREE-00999 freely available EZB journals; Wiley Online Library All Journals |
| subjects | Adaptor Proteins, Signal Transducing - genetics Adaptor Proteins, Signal Transducing - metabolism Alkyl and Aryl Transferases - genetics Alkyl and Aryl Transferases - metabolism Animals Anthers Arabidopsis Arabidopsis - genetics Arabidopsis - metabolism Arabidopsis Proteins - genetics Arabidopsis Proteins - metabolism Arabidopsis thaliana Binding Deuterium Fertility Geranylgeranyltransferase HDX‐MS Hydrogen-deuterium exchange Lipid bilayers Lipids Male sterility Mass spectrometry Mass spectroscopy Original Plant Infertility Pollen Protein Binding protein geranylgeranylation Protein Prenylation Protein Processing, Post-Translational Proteins Rab escort protein rab GTP-Binding Proteins - genetics rab GTP-Binding Proteins - metabolism Rab proteins Yeast Yeasts |
| title | Impact of C‐terminal truncations in the Arabidopsis Rab escort protein (REP) on REP–Rab interaction and plant fertility |
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