Paramagnetic Relaxation Enhancement Reveals Oligomerization Interface of a Membrane Protein

Protein–protein interactions play critical roles in cellular function and oligomerization of membrane proteins is a commonly observed phenomenon. Determining the oligomerization state and defining the intermolecular interface in the bilayer is generally a difficult task. Here, we use site-specific s...

Full description

Saved in:
Bibliographic Details
Published in:Journal of the American Chemical Society 2012-10, Vol.134 (41), p.16995-16998
Main Authors: Wang, Shenlin, Munro, Rachel A, Kim, So Young, Jung, Kwang-Hwan, Brown, Leonid S, Ladizhansky, Vladimir
Format: Article
Language:English
Subjects:
Anabaena - chemistry
Sensory Rhodopsins - chemistry
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
cited_by cdi_FETCH-LOGICAL-a381t-c2840018673c41f2a19b8eb4ac8f9f473921cd4769790ebce34d8c42587688133
cites cdi_FETCH-LOGICAL-a381t-c2840018673c41f2a19b8eb4ac8f9f473921cd4769790ebce34d8c42587688133
container_end_page 16998
container_issue 41
container_start_page 16995
container_title Journal of the American Chemical Society
container_volume 134
creator Wang, Shenlin
Munro, Rachel A
Kim, So Young
Jung, Kwang-Hwan
Brown, Leonid S
Ladizhansky, Vladimir
description Protein–protein interactions play critical roles in cellular function and oligomerization of membrane proteins is a commonly observed phenomenon. Determining the oligomerization state and defining the intermolecular interface in the bilayer is generally a difficult task. Here, we use site-specific spin labeling to demonstrate that relaxation enhancements induced by covalently attached paramagnetic tag can provide distance restraints defining the intermonomer interface in oligomers formed by a seven-helical transmembrane protein Anabaena Sensory Rhodopsin (ASR). We combine these measurements with visible CD spectroscopy and cross-linking experiments to demonstrate that ASR forms tight trimers in both detergents and lipids.
doi_str_mv 10.1021/ja308310z
format article
fullrecord <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_1113214686</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>1113214686</sourcerecordid><originalsourceid>FETCH-LOGICAL-a381t-c2840018673c41f2a19b8eb4ac8f9f473921cd4769790ebce34d8c42587688133</originalsourceid><addsrcrecordid>eNptkDFPwzAQhS0EoqUw8AdQFiQYAj7bTZwRVQUqFbVCMDFEjnspqRK72AmC_nqMWjoxne70vad7j5BzoDdAGdyuFKeSA90ckD4MGY2HwJJD0qeUsjiVCe-RE-9XYRVMwjHpMU6DAnifvM2VU41aGmwrHT1jrb5UW1kTjc27MhobNG04f6KqfTSrq6Vt0FWbLTMxLbpSaYxsGanoCZvCKYPR3NkWK3NKjsogw7PdHJDX-_HL6DGezh4mo7tprLiENtZMCkpBJinXAkqmICskFkJpWWalSHnGQC9EmmRpRrHQyMVCasGGMk1kCMEH5Grru3b2o0Pf5k3lNdZ1-MV2PgcAzkAkoYgBud6i2lnvHZb52lWNct850Py3y3zfZWAvdrZd0eBiT_6VF4DLLaC0z1e2cyak_MfoB28oejs</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1113214686</pqid></control><display><type>article</type><title>Paramagnetic Relaxation Enhancement Reveals Oligomerization Interface of a Membrane Protein</title><source>American Chemical Society:Jisc Collections:American Chemical Society Read &amp; Publish Agreement 2022-2024 (Reading list)</source><creator>Wang, Shenlin ; Munro, Rachel A ; Kim, So Young ; Jung, Kwang-Hwan ; Brown, Leonid S ; Ladizhansky, Vladimir</creator><creatorcontrib>Wang, Shenlin ; Munro, Rachel A ; Kim, So Young ; Jung, Kwang-Hwan ; Brown, Leonid S ; Ladizhansky, Vladimir</creatorcontrib><description>Protein–protein interactions play critical roles in cellular function and oligomerization of membrane proteins is a commonly observed phenomenon. Determining the oligomerization state and defining the intermolecular interface in the bilayer is generally a difficult task. Here, we use site-specific spin labeling to demonstrate that relaxation enhancements induced by covalently attached paramagnetic tag can provide distance restraints defining the intermonomer interface in oligomers formed by a seven-helical transmembrane protein Anabaena Sensory Rhodopsin (ASR). We combine these measurements with visible CD spectroscopy and cross-linking experiments to demonstrate that ASR forms tight trimers in both detergents and lipids.</description><identifier>ISSN: 0002-7863</identifier><identifier>EISSN: 1520-5126</identifier><identifier>DOI: 10.1021/ja308310z</identifier><identifier>PMID: 23030813</identifier><language>eng</language><publisher>United States: American Chemical Society</publisher><subject>Anabaena - chemistry ; Sensory Rhodopsins - chemistry</subject><ispartof>Journal of the American Chemical Society, 2012-10, Vol.134 (41), p.16995-16998</ispartof><rights>Copyright © 2012 American Chemical Society</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a381t-c2840018673c41f2a19b8eb4ac8f9f473921cd4769790ebce34d8c42587688133</citedby><cites>FETCH-LOGICAL-a381t-c2840018673c41f2a19b8eb4ac8f9f473921cd4769790ebce34d8c42587688133</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/23030813$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Wang, Shenlin</creatorcontrib><creatorcontrib>Munro, Rachel A</creatorcontrib><creatorcontrib>Kim, So Young</creatorcontrib><creatorcontrib>Jung, Kwang-Hwan</creatorcontrib><creatorcontrib>Brown, Leonid S</creatorcontrib><creatorcontrib>Ladizhansky, Vladimir</creatorcontrib><title>Paramagnetic Relaxation Enhancement Reveals Oligomerization Interface of a Membrane Protein</title><title>Journal of the American Chemical Society</title><addtitle>J. Am. Chem. Soc</addtitle><description>Protein–protein interactions play critical roles in cellular function and oligomerization of membrane proteins is a commonly observed phenomenon. Determining the oligomerization state and defining the intermolecular interface in the bilayer is generally a difficult task. Here, we use site-specific spin labeling to demonstrate that relaxation enhancements induced by covalently attached paramagnetic tag can provide distance restraints defining the intermonomer interface in oligomers formed by a seven-helical transmembrane protein Anabaena Sensory Rhodopsin (ASR). We combine these measurements with visible CD spectroscopy and cross-linking experiments to demonstrate that ASR forms tight trimers in both detergents and lipids.</description><subject>Anabaena - chemistry</subject><subject>Sensory Rhodopsins - chemistry</subject><issn>0002-7863</issn><issn>1520-5126</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><recordid>eNptkDFPwzAQhS0EoqUw8AdQFiQYAj7bTZwRVQUqFbVCMDFEjnspqRK72AmC_nqMWjoxne70vad7j5BzoDdAGdyuFKeSA90ckD4MGY2HwJJD0qeUsjiVCe-RE-9XYRVMwjHpMU6DAnifvM2VU41aGmwrHT1jrb5UW1kTjc27MhobNG04f6KqfTSrq6Vt0FWbLTMxLbpSaYxsGanoCZvCKYPR3NkWK3NKjsogw7PdHJDX-_HL6DGezh4mo7tprLiENtZMCkpBJinXAkqmICskFkJpWWalSHnGQC9EmmRpRrHQyMVCasGGMk1kCMEH5Grru3b2o0Pf5k3lNdZ1-MV2PgcAzkAkoYgBud6i2lnvHZb52lWNct850Py3y3zfZWAvdrZd0eBiT_6VF4DLLaC0z1e2cyak_MfoB28oejs</recordid><startdate>20121017</startdate><enddate>20121017</enddate><creator>Wang, Shenlin</creator><creator>Munro, Rachel A</creator><creator>Kim, So Young</creator><creator>Jung, Kwang-Hwan</creator><creator>Brown, Leonid S</creator><creator>Ladizhansky, Vladimir</creator><general>American Chemical Society</general><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>7X8</scope></search><sort><creationdate>20121017</creationdate><title>Paramagnetic Relaxation Enhancement Reveals Oligomerization Interface of a Membrane Protein</title><author>Wang, Shenlin ; Munro, Rachel A ; Kim, So Young ; Jung, Kwang-Hwan ; Brown, Leonid S ; Ladizhansky, Vladimir</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a381t-c2840018673c41f2a19b8eb4ac8f9f473921cd4769790ebce34d8c42587688133</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>Anabaena - chemistry</topic><topic>Sensory Rhodopsins - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Wang, Shenlin</creatorcontrib><creatorcontrib>Munro, Rachel A</creatorcontrib><creatorcontrib>Kim, So Young</creatorcontrib><creatorcontrib>Jung, Kwang-Hwan</creatorcontrib><creatorcontrib>Brown, Leonid S</creatorcontrib><creatorcontrib>Ladizhansky, Vladimir</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of the American Chemical Society</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Wang, Shenlin</au><au>Munro, Rachel A</au><au>Kim, So Young</au><au>Jung, Kwang-Hwan</au><au>Brown, Leonid S</au><au>Ladizhansky, Vladimir</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Paramagnetic Relaxation Enhancement Reveals Oligomerization Interface of a Membrane Protein</atitle><jtitle>Journal of the American Chemical Society</jtitle><addtitle>J. Am. Chem. Soc</addtitle><date>2012-10-17</date><risdate>2012</risdate><volume>134</volume><issue>41</issue><spage>16995</spage><epage>16998</epage><pages>16995-16998</pages><issn>0002-7863</issn><eissn>1520-5126</eissn><abstract>Protein–protein interactions play critical roles in cellular function and oligomerization of membrane proteins is a commonly observed phenomenon. Determining the oligomerization state and defining the intermolecular interface in the bilayer is generally a difficult task. Here, we use site-specific spin labeling to demonstrate that relaxation enhancements induced by covalently attached paramagnetic tag can provide distance restraints defining the intermonomer interface in oligomers formed by a seven-helical transmembrane protein Anabaena Sensory Rhodopsin (ASR). We combine these measurements with visible CD spectroscopy and cross-linking experiments to demonstrate that ASR forms tight trimers in both detergents and lipids.</abstract><cop>United States</cop><pub>American Chemical Society</pub><pmid>23030813</pmid><doi>10.1021/ja308310z</doi><tpages>4</tpages></addata></record>
fulltext fulltext
identifier ISSN: 0002-7863
ispartof Journal of the American Chemical Society, 2012-10, Vol.134 (41), p.16995-16998
issn 0002-7863
1520-5126
language eng
recordid cdi_proquest_miscellaneous_1113214686
source American Chemical Society:Jisc Collections:American Chemical Society Read & Publish Agreement 2022-2024 (Reading list)
subjects Anabaena - chemistry
Sensory Rhodopsins - chemistry
title Paramagnetic Relaxation Enhancement Reveals Oligomerization Interface of a Membrane Protein
url http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-23T12%3A42%3A26IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Paramagnetic%20Relaxation%20Enhancement%20Reveals%20Oligomerization%20Interface%20of%20a%20Membrane%20Protein&rft.jtitle=Journal%20of%20the%20American%20Chemical%20Society&rft.au=Wang,%20Shenlin&rft.date=2012-10-17&rft.volume=134&rft.issue=41&rft.spage=16995&rft.epage=16998&rft.pages=16995-16998&rft.issn=0002-7863&rft.eissn=1520-5126&rft_id=info:doi/10.1021/ja308310z&rft_dat=%3Cproquest_cross%3E1113214686%3C/proquest_cross%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-a381t-c2840018673c41f2a19b8eb4ac8f9f473921cd4769790ebce34d8c42587688133%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=1113214686&rft_id=info:pmid/23030813&rfr_iscdi=true