Molecular Characterization of Helix-Loop-Helix Peptides
A class of regulators of eokaryotic gene expression contains a conserved amino acid sequence responsible for protein oligomerization and binding to DNA. This structure consists of an arginine- and lysine-rich basic region followed by a helix-loop-helix motif, which together mediate specific binding...
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| Veröffentlicht in: | Science (American Association for the Advancement of Science) 1992-02, Vol.255 (5047), p.979-983 |
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| container_issue | 5047 |
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| container_title | Science (American Association for the Advancement of Science) |
| container_volume | 255 |
| creator | Anthony-Cahill, Spencer J. Benfield, Pamela A. Fairman, Robert Wasserman, Zelda R. Brenner, Stephen L. Stafford, Walter F. Altenbach, Christian Hubbell, Wayne L. DeGrado, William F. |
| description | A class of regulators of eokaryotic gene expression contains a conserved amino acid sequence responsible for protein oligomerization and binding to DNA. This structure consists of an arginine- and lysine-rich basic region followed by a helix-loop-helix motif, which together mediate specific binding to DNA. Peptides were prepared that span this motif in the MyoD protein; in solution, they formed α-helical dimers and tetramers. They bound to DNA as dimers and their α-helical content increased on binding. Parallel and antiparallel four-helix models of the DNA-bound dimer were constructed. Peptides containing disulfide bonds were engineered to test the correctness of the two models. A disulfide that is compatible with the parallel model promotes specific interaction with DNA, whereas a disulfide compatible with the antiparallel model abolishes specific binding. Electron paramagnetic resonance (EPR) measurements of nitroxide-labeled peptides provided intersubunit distance measurements that also supported the parallel model. |
| doi_str_mv | 10.1126/science.1312255 |
| format | Article |
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Psychology ; Gene Expression Regulation ; Humans ; Models, Molecular ; Molecular Sequence Data ; Molecular structure ; Monomers ; Mops ; Peptides ; Protein Conformation ; Protein structure ; Proteins ; Regulatory Sequences, Nucleic Acid ; Sequence Alignment ; Spin labels ; Structure ; Transcription Factors - chemistry</subject><ispartof>Science (American Association for the Advancement of Science), 1992-02, Vol.255 (5047), p.979-983</ispartof><rights>Copyright 1992 American Association for the Advancement of Science</rights><rights>1992 INIST-CNRS</rights><rights>COPYRIGHT 1992 American Association for the Advancement of Science</rights><rights>COPYRIGHT 1992 American Association for the Advancement of Science</rights><rights>Copyright American Association for the Advancement of Science Feb 21, 1992</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c706t-d44534506488504709891a57cd26aef49ca74b23592c405c4e42bc3beb3dc46e3</citedby><cites>FETCH-LOGICAL-c706t-d44534506488504709891a57cd26aef49ca74b23592c405c4e42bc3beb3dc46e3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/2876590$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/2876590$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>314,776,780,799,2871,2872,27901,27902,57992,58225</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=5207429$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1312255$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Anthony-Cahill, Spencer J.</creatorcontrib><creatorcontrib>Benfield, Pamela A.</creatorcontrib><creatorcontrib>Fairman, Robert</creatorcontrib><creatorcontrib>Wasserman, Zelda R.</creatorcontrib><creatorcontrib>Brenner, Stephen L.</creatorcontrib><creatorcontrib>Stafford, Walter F.</creatorcontrib><creatorcontrib>Altenbach, Christian</creatorcontrib><creatorcontrib>Hubbell, Wayne L.</creatorcontrib><creatorcontrib>DeGrado, William F.</creatorcontrib><title>Molecular Characterization of Helix-Loop-Helix Peptides</title><title>Science (American Association for the Advancement of Science)</title><addtitle>Science</addtitle><description>A class of regulators of eokaryotic gene expression contains a conserved amino acid sequence responsible for protein oligomerization and binding to DNA. 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Electron paramagnetic resonance (EPR) measurements of nitroxide-labeled peptides provided intersubunit distance measurements that also supported the parallel model.</description><subject>Amino Acid Sequence</subject><subject>Amino acids</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Binding and carrier proteins</subject><subject>Binding Sites</subject><subject>Biochemistry</subject><subject>Biological and medical sciences</subject><subject>Cellular biology</subject><subject>Circular Dichroism</subject><subject>Deoxyribonucleic acid</subject><subject>Dimers</subject><subject>Disulfides</subject><subject>DNA</subject><subject>DNA-Binding Proteins - chemistry</subject><subject>Drug interactions</subject><subject>Electron paramagnetic resonance spectroscopy</subject><subject>Electron Spin Resonance Spectroscopy</subject><subject>Enhancer Elements, Genetic</subject><subject>Fractions</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene Expression Regulation</subject><subject>Humans</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Molecular structure</subject><subject>Monomers</subject><subject>Mops</subject><subject>Peptides</subject><subject>Protein Conformation</subject><subject>Protein structure</subject><subject>Proteins</subject><subject>Regulatory Sequences, Nucleic Acid</subject><subject>Sequence Alignment</subject><subject>Spin labels</subject><subject>Structure</subject><subject>Transcription Factors - chemistry</subject><issn>0036-8075</issn><issn>1095-9203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>BEC</sourceid><sourceid>BENPR</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNqN0s1v0zAUAPAIgUYZnLmAVE0IOCybP-P4OCroJhWKxMfVcpyX4sqNi51I2_56XBoVFVVQ-WDL7-ev55dlzzG6wJgUl9FYaA1cYIoJ4fxBNsJI8lwSRB9mI4RokZdI8MfZkxiXCKWYpCfZycBHmfjoHZje6TCe_NBBmw6Cvded9e3YN-NrcPY2n3m_zn8Px59h3dka4tPsUaNdhGdDf5p9-_D-6-Q6n82nN5OrWW4EKrq8ZoxTxlHBypIjJpAsJdZcmJoUGhomjRasIpRLYhjihgEjlaEVVLQ2rAB6mr3Z7rsO_mcPsVMrGw04p1vwfVSCUSIRwjTJ1_-WpEx3Qey_EBckZU8UCZ79BZe-D216riKYco4E2aDzLVpoB8q2je9SFhfQQtDOt9DYNH2FsSxKwTeH5wd4ajWsrDnk3-75RDq47Ra6j1HdfPl0NJ1_P5q-mx5Ly-lsj54fosY7BwtQqS4m8z1-ueUm-BgDNGod7EqHO4WR2hS3GopbDdWaVrwcPqSvVlD_8bv4qyGuo9GuCbo1Nu4YJ0gwIhN7sWXL2PmwC5NSFFwi-gtytQRb</recordid><startdate>19920221</startdate><enddate>19920221</enddate><creator>Anthony-Cahill, Spencer J.</creator><creator>Benfield, Pamela A.</creator><creator>Fairman, Robert</creator><creator>Wasserman, Zelda R.</creator><creator>Brenner, Stephen L.</creator><creator>Stafford, Walter F.</creator><creator>Altenbach, Christian</creator><creator>Hubbell, Wayne L.</creator><creator>DeGrado, William F.</creator><general>American Society for the Advancement of Science</general><general>American Association for the Advancement of Science</general><general>The American Association for the Advancement of Science</general><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>8GL</scope><scope>IBG</scope><scope>IOV</scope><scope>ISN</scope><scope>0-V</scope><scope>3V.</scope><scope>7QF</scope><scope>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QQ</scope><scope>7QR</scope><scope>7SC</scope><scope>7SE</scope><scope>7SN</scope><scope>7SP</scope><scope>7SR</scope><scope>7SS</scope><scope>7T7</scope><scope>7TA</scope><scope>7TB</scope><scope>7TK</scope><scope>7TM</scope><scope>7U5</scope><scope>7U9</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88B</scope><scope>88E</scope><scope>88I</scope><scope>8AF</scope><scope>8BQ</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>ALSLI</scope><scope>ARAPS</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BEC</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>BKSAR</scope><scope>C1K</scope><scope>CCPQU</scope><scope>CJNVE</scope><scope>D1I</scope><scope>DWQXO</scope><scope>F28</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H8D</scope><scope>H8G</scope><scope>H94</scope><scope>HCIFZ</scope><scope>JG9</scope><scope>JQ2</scope><scope>K9-</scope><scope>K9.</scope><scope>KB.</scope><scope>KR7</scope><scope>L6V</scope><scope>L7M</scope><scope>LK8</scope><scope>L~C</scope><scope>L~D</scope><scope>M0K</scope><scope>M0P</scope><scope>M0R</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>M7S</scope><scope>MBDVC</scope><scope>P5Z</scope><scope>P62</scope><scope>P64</scope><scope>PATMY</scope><scope>PCBAR</scope><scope>PDBOC</scope><scope>PQEDU</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>PTHSS</scope><scope>PYCSY</scope><scope>Q9U</scope><scope>R05</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>19920221</creationdate><title>Molecular Characterization of Helix-Loop-Helix Peptides</title><author>Anthony-Cahill, Spencer J. ; 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Psychology</topic><topic>Gene Expression Regulation</topic><topic>Humans</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>Molecular structure</topic><topic>Monomers</topic><topic>Mops</topic><topic>Peptides</topic><topic>Protein Conformation</topic><topic>Protein structure</topic><topic>Proteins</topic><topic>Regulatory Sequences, Nucleic Acid</topic><topic>Sequence Alignment</topic><topic>Spin labels</topic><topic>Structure</topic><topic>Transcription Factors - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Anthony-Cahill, Spencer J.</creatorcontrib><creatorcontrib>Benfield, Pamela A.</creatorcontrib><creatorcontrib>Fairman, Robert</creatorcontrib><creatorcontrib>Wasserman, Zelda R.</creatorcontrib><creatorcontrib>Brenner, Stephen L.</creatorcontrib><creatorcontrib>Stafford, Walter F.</creatorcontrib><creatorcontrib>Altenbach, Christian</creatorcontrib><creatorcontrib>Hubbell, Wayne 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This structure consists of an arginine- and lysine-rich basic region followed by a helix-loop-helix motif, which together mediate specific binding to DNA. Peptides were prepared that span this motif in the MyoD protein; in solution, they formed α-helical dimers and tetramers. They bound to DNA as dimers and their α-helical content increased on binding. Parallel and antiparallel four-helix models of the DNA-bound dimer were constructed. Peptides containing disulfide bonds were engineered to test the correctness of the two models. A disulfide that is compatible with the parallel model promotes specific interaction with DNA, whereas a disulfide compatible with the antiparallel model abolishes specific binding. Electron paramagnetic resonance (EPR) measurements of nitroxide-labeled peptides provided intersubunit distance measurements that also supported the parallel model.</abstract><cop>Washington, DC</cop><pub>American Society for the Advancement of Science</pub><pmid>1312255</pmid><doi>10.1126/science.1312255</doi><tpages>5</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0036-8075 |
| ispartof | Science (American Association for the Advancement of Science), 1992-02, Vol.255 (5047), p.979-983 |
| issn | 0036-8075 1095-9203 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_743290013 |
| source | American Association for the Advancement of Science; Jstor Complete Legacy; MEDLINE |
| subjects | Amino Acid Sequence Amino acids Analytical, structural and metabolic biochemistry Animals Binding and carrier proteins Binding Sites Biochemistry Biological and medical sciences Cellular biology Circular Dichroism Deoxyribonucleic acid Dimers Disulfides DNA DNA-Binding Proteins - chemistry Drug interactions Electron paramagnetic resonance spectroscopy Electron Spin Resonance Spectroscopy Enhancer Elements, Genetic Fractions Fundamental and applied biological sciences. Psychology Gene Expression Regulation Humans Models, Molecular Molecular Sequence Data Molecular structure Monomers Mops Peptides Protein Conformation Protein structure Proteins Regulatory Sequences, Nucleic Acid Sequence Alignment Spin labels Structure Transcription Factors - chemistry |
| title | Molecular Characterization of Helix-Loop-Helix Peptides |
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