Structural organization of the human eukaryotic initiation factor 5A precursor and its site-directed variant Lys50-->Arg
The molecular properties of the human eukaryotic initiation factor 5A precursor and its site directed Lys50-->Arg variant have been investigated and compared. Structure perturbation methods were used to gain information about the protein architecture in solution. Intrinsic and extrinsic spectrosc...
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| Veröffentlicht in: | Amino acids 1999-01, Vol.16 (1), p.91-106 |
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| creator | Stiuso, P Colonna, G Ragone, R Caraglia, M Hershey, J W Beninati, S Abbruzzese, A |
| description | The molecular properties of the human eukaryotic initiation factor 5A precursor and its site directed Lys50-->Arg variant have been investigated and compared. Structure perturbation methods were used to gain information about the protein architecture in solution. Intrinsic and extrinsic spectroscopic probes strategically located in the protein matrix detected the independent unfolding of two molecular regions. Three cysteines out of four were titrated in the native protein and the peculiar presence of a tyrosinate band at neutral pH was detected. At alkaline pH only two tyrosines out of three were titratable in the native protein, with an apparent pK of about 9.9. Native protein and its Lys50-->Arg variant reacted in a similar fashion to guanidine and to pH variation, but differently to thermal stress. The complex thermal unfolding of both proteins indicated the presence of intermediates. Spectroscopic data showed that these intermediates are differently structured. Consequently, the two proteins seem to have different unfolding pathways. |
| doi_str_mv | 10.1007/BF01318888 |
| format | Article |
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Structure perturbation methods were used to gain information about the protein architecture in solution. Intrinsic and extrinsic spectroscopic probes strategically located in the protein matrix detected the independent unfolding of two molecular regions. Three cysteines out of four were titrated in the native protein and the peculiar presence of a tyrosinate band at neutral pH was detected. At alkaline pH only two tyrosines out of three were titratable in the native protein, with an apparent pK of about 9.9. Native protein and its Lys50-->Arg variant reacted in a similar fashion to guanidine and to pH variation, but differently to thermal stress. The complex thermal unfolding of both proteins indicated the presence of intermediates. Spectroscopic data showed that these intermediates are differently structured. Consequently, the two proteins seem to have different unfolding pathways.</description><identifier>ISSN: 0939-4451</identifier><identifier>EISSN: 1438-2199</identifier><identifier>DOI: 10.1007/BF01318888</identifier><identifier>PMID: 10078337</identifier><language>eng</language><publisher>Austria: Springer Nature B.V</publisher><subject>Amino Acid Substitution ; Arginine - chemistry ; Base Sequence ; Chemistry ; Circular Dichroism ; DNA Primers ; Eukaryotic Translation Initiation Factor 5A ; Fluorescent Dyes ; Guanidine - chemistry ; Humans ; Lysine - chemistry ; Mutagenesis, Site-Directed ; Naphthalenesulfonates ; Peptide Initiation Factors - chemistry ; Peptide Initiation Factors - genetics ; Protein Conformation ; Protein Denaturation ; Protein folding ; Protein Precursors - chemistry ; Protein Precursors - genetics ; RNA-Binding Proteins ; Spectrophotometry, Ultraviolet</subject><ispartof>Amino acids, 1999-01, Vol.16 (1), p.91-106</ispartof><rights>Springer-Verlag 1999</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c311t-1a0807744a1e30fba8d466b32acfc89c376e8157b7916e7d1162dcbbdc122d183</citedby><cites>FETCH-LOGICAL-c311t-1a0807744a1e30fba8d466b32acfc89c376e8157b7916e7d1162dcbbdc122d183</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>315,782,786,27933,27934</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10078337$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Stiuso, P</creatorcontrib><creatorcontrib>Colonna, G</creatorcontrib><creatorcontrib>Ragone, R</creatorcontrib><creatorcontrib>Caraglia, M</creatorcontrib><creatorcontrib>Hershey, J W</creatorcontrib><creatorcontrib>Beninati, S</creatorcontrib><creatorcontrib>Abbruzzese, A</creatorcontrib><title>Structural organization of the human eukaryotic initiation factor 5A precursor and its site-directed variant Lys50-->Arg</title><title>Amino acids</title><addtitle>Amino Acids</addtitle><description>The molecular properties of the human eukaryotic initiation factor 5A precursor and its site directed Lys50-->Arg variant have been investigated and compared. Structure perturbation methods were used to gain information about the protein architecture in solution. Intrinsic and extrinsic spectroscopic probes strategically located in the protein matrix detected the independent unfolding of two molecular regions. Three cysteines out of four were titrated in the native protein and the peculiar presence of a tyrosinate band at neutral pH was detected. At alkaline pH only two tyrosines out of three were titratable in the native protein, with an apparent pK of about 9.9. Native protein and its Lys50-->Arg variant reacted in a similar fashion to guanidine and to pH variation, but differently to thermal stress. The complex thermal unfolding of both proteins indicated the presence of intermediates. Spectroscopic data showed that these intermediates are differently structured. Consequently, the two proteins seem to have different unfolding pathways.</description><subject>Amino Acid Substitution</subject><subject>Arginine - chemistry</subject><subject>Base Sequence</subject><subject>Chemistry</subject><subject>Circular Dichroism</subject><subject>DNA Primers</subject><subject>Eukaryotic Translation Initiation Factor 5A</subject><subject>Fluorescent Dyes</subject><subject>Guanidine - chemistry</subject><subject>Humans</subject><subject>Lysine - chemistry</subject><subject>Mutagenesis, Site-Directed</subject><subject>Naphthalenesulfonates</subject><subject>Peptide Initiation Factors - chemistry</subject><subject>Peptide Initiation Factors - genetics</subject><subject>Protein Conformation</subject><subject>Protein Denaturation</subject><subject>Protein folding</subject><subject>Protein Precursors - chemistry</subject><subject>Protein Precursors - genetics</subject><subject>RNA-Binding Proteins</subject><subject>Spectrophotometry, Ultraviolet</subject><issn>0939-4451</issn><issn>1438-2199</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNpNkEtLAzEQgIMotj4u_gAJeBNWM5vdTfYi1GJVKHhQz0s2ybap7abmIdZfb0oLOpdhhm9mmA-hCyA3QAi7vZ8QoMBTHKAhFJRnOdT1IRqSmtZZUZQwQCfeLwiBnEN1jAbbMU4pG6Lv1-CiDNGJJbZuJnrzI4KxPbYdDnON53Eleqzjh3AbG4zEpjfB7JBOyGAdLkd47bSMzqdC9Aqb4LE3QWfKpH7QCn8JZ0Qf8HTjS5JldyM3O0NHnVh6fb7Pp-h98vA2fsqmL4_P49E0kxQgZCAIJ4wVhQBNSdcKroqqamkuZCd5LSmrNIeStayGSjMFUOVKtq2SkOcKOD1FV7u9a2c_o_ahWdjo-nSyAVKXbCsuT9T1jpLOeu9016ydWaWfE9RsbTV_khN8uV8Z25VW_9CdVfoLaHB3Rw</recordid><startdate>19990101</startdate><enddate>19990101</enddate><creator>Stiuso, P</creator><creator>Colonna, G</creator><creator>Ragone, R</creator><creator>Caraglia, M</creator><creator>Hershey, J W</creator><creator>Beninati, S</creator><creator>Abbruzzese, A</creator><general>Springer Nature B.V</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>3V.</scope><scope>7TK</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>D1I</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>KB.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7P</scope><scope>PDBOC</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope></search><sort><creationdate>19990101</creationdate><title>Structural organization of the human eukaryotic initiation factor 5A precursor and its site-directed variant Lys50-->Arg</title><author>Stiuso, P ; Colonna, G ; Ragone, R ; Caraglia, M ; Hershey, J W ; Beninati, S ; Abbruzzese, A</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c311t-1a0807744a1e30fba8d466b32acfc89c376e8157b7916e7d1162dcbbdc122d183</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1999</creationdate><topic>Amino Acid Substitution</topic><topic>Arginine - chemistry</topic><topic>Base Sequence</topic><topic>Chemistry</topic><topic>Circular Dichroism</topic><topic>DNA Primers</topic><topic>Eukaryotic Translation Initiation Factor 5A</topic><topic>Fluorescent Dyes</topic><topic>Guanidine - chemistry</topic><topic>Humans</topic><topic>Lysine - chemistry</topic><topic>Mutagenesis, Site-Directed</topic><topic>Naphthalenesulfonates</topic><topic>Peptide Initiation Factors - chemistry</topic><topic>Peptide Initiation Factors - genetics</topic><topic>Protein Conformation</topic><topic>Protein Denaturation</topic><topic>Protein folding</topic><topic>Protein Precursors - chemistry</topic><topic>Protein Precursors - genetics</topic><topic>RNA-Binding Proteins</topic><topic>Spectrophotometry, Ultraviolet</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Stiuso, P</creatorcontrib><creatorcontrib>Colonna, G</creatorcontrib><creatorcontrib>Ragone, R</creatorcontrib><creatorcontrib>Caraglia, M</creatorcontrib><creatorcontrib>Hershey, J W</creatorcontrib><creatorcontrib>Beninati, S</creatorcontrib><creatorcontrib>Abbruzzese, A</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Neurosciences Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Materials Science & Engineering Collection</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Technology Collection</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Materials Science Collection</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Materials Science Database</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Biological Science Database</collection><collection>Materials Science Collection</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><jtitle>Amino acids</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Stiuso, P</au><au>Colonna, G</au><au>Ragone, R</au><au>Caraglia, M</au><au>Hershey, J W</au><au>Beninati, S</au><au>Abbruzzese, A</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structural organization of the human eukaryotic initiation factor 5A precursor and its site-directed variant Lys50-->Arg</atitle><jtitle>Amino acids</jtitle><addtitle>Amino Acids</addtitle><date>1999-01-01</date><risdate>1999</risdate><volume>16</volume><issue>1</issue><spage>91</spage><epage>106</epage><pages>91-106</pages><issn>0939-4451</issn><eissn>1438-2199</eissn><abstract>The molecular properties of the human eukaryotic initiation factor 5A precursor and its site directed Lys50-->Arg variant have been investigated and compared. Structure perturbation methods were used to gain information about the protein architecture in solution. Intrinsic and extrinsic spectroscopic probes strategically located in the protein matrix detected the independent unfolding of two molecular regions. Three cysteines out of four were titrated in the native protein and the peculiar presence of a tyrosinate band at neutral pH was detected. At alkaline pH only two tyrosines out of three were titratable in the native protein, with an apparent pK of about 9.9. Native protein and its Lys50-->Arg variant reacted in a similar fashion to guanidine and to pH variation, but differently to thermal stress. The complex thermal unfolding of both proteins indicated the presence of intermediates. Spectroscopic data showed that these intermediates are differently structured. Consequently, the two proteins seem to have different unfolding pathways.</abstract><cop>Austria</cop><pub>Springer Nature B.V</pub><pmid>10078337</pmid><doi>10.1007/BF01318888</doi><tpages>16</tpages></addata></record> |
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| ispartof | Amino acids, 1999-01, Vol.16 (1), p.91-106 |
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| subjects | Amino Acid Substitution Arginine - chemistry Base Sequence Chemistry Circular Dichroism DNA Primers Eukaryotic Translation Initiation Factor 5A Fluorescent Dyes Guanidine - chemistry Humans Lysine - chemistry Mutagenesis, Site-Directed Naphthalenesulfonates Peptide Initiation Factors - chemistry Peptide Initiation Factors - genetics Protein Conformation Protein Denaturation Protein folding Protein Precursors - chemistry Protein Precursors - genetics RNA-Binding Proteins Spectrophotometry, Ultraviolet |
| title | Structural organization of the human eukaryotic initiation factor 5A precursor and its site-directed variant Lys50-->Arg |
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