Interaction of thioredoxins with target proteins: Role of particular structural elements and electrostatic properties of thioredoxins in their interplay with 2-oxoacid dehydrogenase complexes
The thioredoxin action upon the 2-oxoacid dehydrogenase complexes is investigated by using different thioredoxins, both wild-type and mutated. The attacking cysteine residue of thioredoxin is established to be essential for the thioredoxin-dependent activation of the complexes. Mutation of the burie...
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| Veröffentlicht in: | Protein science 1999-01, Vol.8 (1), p.65-74 |
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| creator | BUNIK, VICTORIA RADDATZ, GÜNTER LEMAIRE, STEPHANE MEYER, YVES JACQUOT, JEAN-PIERRE BISSWANGER, HANS |
| description | The thioredoxin action upon the 2-oxoacid dehydrogenase
complexes is investigated by using different thioredoxins,
both wild-type and mutated. The attacking cysteine residue
of thioredoxin is established to be essential for the thioredoxin-dependent
activation of the complexes. Mutation of the buried cysteine
residue to serine is not crucial for the activation, but
prevents inhibition of the complexes, exhibited by the
Clamydomonas reinhardtii thioredoxin m
disulfide. Site-directed mutagenesis of D26, W31, F/W12,
and Y/A70 (the Escherichia coli thioredoxin numbering
is employed for all the thioredoxins studied) indicates
that both the active site and remote residues of thioredoxin
are involved in its interplay with the 2-oxoacid dehydrogenase
complexes. Sequences of 11 thioredoxin species tested biochemically
are aligned. The thioredoxin residues at the contact between
the α3/310 and α1 helices, the length
of the α1 helix and the charges in the α2-β3
and β4-β5 linkers are found to correlate with the
protein influence on the 2-oxoacid dehydrogenase complexes
(the secondary structural elements of thioredoxin are defined
according to Eklund H et al., 1991, Proteins 11:13–28).
The distribution of the charges on the surface of the thioredoxin
molecules is analyzed. The analysis reveals the species
specific polarization of the thioredoxin active site surroundings,
which corresponds to the efficiency of the thioredoxin
interplay with the 2-oxoacid dehydrogenase systems. The
most effective mitochondrial thioredoxin is characterized
by the strongest polarization of this area and the highest
value of the electrostatic dipole vector of the molecule.
Not only the magnitude, but also the orientation of the
dipole vector show correlation with the thioredoxin action.
The dipole direction is found to be significantly influenced
by the charges of the residues 13/14, 51, and 83/85, which
distinguish the activating and inhibiting thioredoxin disulfides. |
| doi_str_mv | 10.1110/ps.8.1.65 |
| format | Article |
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complexes is investigated by using different thioredoxins,
both wild-type and mutated. The attacking cysteine residue
of thioredoxin is established to be essential for the thioredoxin-dependent
activation of the complexes. Mutation of the buried cysteine
residue to serine is not crucial for the activation, but
prevents inhibition of the complexes, exhibited by the
Clamydomonas reinhardtii thioredoxin m
disulfide. Site-directed mutagenesis of D26, W31, F/W12,
and Y/A70 (the Escherichia coli thioredoxin numbering
is employed for all the thioredoxins studied) indicates
that both the active site and remote residues of thioredoxin
are involved in its interplay with the 2-oxoacid dehydrogenase
complexes. Sequences of 11 thioredoxin species tested biochemically
are aligned. The thioredoxin residues at the contact between
the α3/310 and α1 helices, the length
of the α1 helix and the charges in the α2-β3
and β4-β5 linkers are found to correlate with the
protein influence on the 2-oxoacid dehydrogenase complexes
(the secondary structural elements of thioredoxin are defined
according to Eklund H et al., 1991, Proteins 11:13–28).
The distribution of the charges on the surface of the thioredoxin
molecules is analyzed. The analysis reveals the species
specific polarization of the thioredoxin active site surroundings,
which corresponds to the efficiency of the thioredoxin
interplay with the 2-oxoacid dehydrogenase systems. The
most effective mitochondrial thioredoxin is characterized
by the strongest polarization of this area and the highest
value of the electrostatic dipole vector of the molecule.
Not only the magnitude, but also the orientation of the
dipole vector show correlation with the thioredoxin action.
The dipole direction is found to be significantly influenced
by the charges of the residues 13/14, 51, and 83/85, which
distinguish the activating and inhibiting thioredoxin disulfides.</description><identifier>ISSN: 0961-8368</identifier><identifier>EISSN: 1469-896X</identifier><identifier>DOI: 10.1110/ps.8.1.65</identifier><identifier>PMID: 10210184</identifier><language>eng</language><publisher>Bristol: Cambridge University Press</publisher><subject>2‐oxoacid dehydrogenase complex ; 3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide) ; Amino Acid Sequence ; Animals ; Base Sequence ; DNA Primers ; electrostatic dipole vector ; homology modeling ; Ketone Oxidoreductases - metabolism ; long‐range electrostatic interactions ; Molecular Sequence Data ; Multienzyme Complexes - metabolism ; Mutagenesis, Site-Directed ; Protein Binding ; Protein Structure, Secondary ; protein—protein recognition ; Sequence Homology, Amino Acid ; Static Electricity ; structural analog ; thioredoxin ; Thioredoxins - chemistry ; Thioredoxins - genetics ; Thioredoxins - metabolism</subject><ispartof>Protein science, 1999-01, Vol.8 (1), p.65-74</ispartof><rights>1999 The Protein Society</rights><rights>Copyright © 1999 The Protein Society</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4165-ad3b6d7720e10b2028400b7d92179f17264e4230692f8a94f7063ca83f1c2d0e3</citedby><cites>FETCH-LOGICAL-c4165-ad3b6d7720e10b2028400b7d92179f17264e4230692f8a94f7063ca83f1c2d0e3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC2144114/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC2144114/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,724,777,781,882,1412,1428,4010,27904,27905,27906,45555,45556,46390,46814,53772,53774</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10210184$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>BUNIK, VICTORIA</creatorcontrib><creatorcontrib>RADDATZ, GÜNTER</creatorcontrib><creatorcontrib>LEMAIRE, STEPHANE</creatorcontrib><creatorcontrib>MEYER, YVES</creatorcontrib><creatorcontrib>JACQUOT, JEAN-PIERRE</creatorcontrib><creatorcontrib>BISSWANGER, HANS</creatorcontrib><title>Interaction of thioredoxins with target proteins: Role of particular structural elements and electrostatic properties of thioredoxins in their interplay with 2-oxoacid dehydrogenase complexes</title><title>Protein science</title><addtitle>Protein Sci</addtitle><description>The thioredoxin action upon the 2-oxoacid dehydrogenase
complexes is investigated by using different thioredoxins,
both wild-type and mutated. The attacking cysteine residue
of thioredoxin is established to be essential for the thioredoxin-dependent
activation of the complexes. Mutation of the buried cysteine
residue to serine is not crucial for the activation, but
prevents inhibition of the complexes, exhibited by the
Clamydomonas reinhardtii thioredoxin m
disulfide. Site-directed mutagenesis of D26, W31, F/W12,
and Y/A70 (the Escherichia coli thioredoxin numbering
is employed for all the thioredoxins studied) indicates
that both the active site and remote residues of thioredoxin
are involved in its interplay with the 2-oxoacid dehydrogenase
complexes. Sequences of 11 thioredoxin species tested biochemically
are aligned. The thioredoxin residues at the contact between
the α3/310 and α1 helices, the length
of the α1 helix and the charges in the α2-β3
and β4-β5 linkers are found to correlate with the
protein influence on the 2-oxoacid dehydrogenase complexes
(the secondary structural elements of thioredoxin are defined
according to Eklund H et al., 1991, Proteins 11:13–28).
The distribution of the charges on the surface of the thioredoxin
molecules is analyzed. The analysis reveals the species
specific polarization of the thioredoxin active site surroundings,
which corresponds to the efficiency of the thioredoxin
interplay with the 2-oxoacid dehydrogenase systems. The
most effective mitochondrial thioredoxin is characterized
by the strongest polarization of this area and the highest
value of the electrostatic dipole vector of the molecule.
Not only the magnitude, but also the orientation of the
dipole vector show correlation with the thioredoxin action.
The dipole direction is found to be significantly influenced
by the charges of the residues 13/14, 51, and 83/85, which
distinguish the activating and inhibiting thioredoxin disulfides.</description><subject>2‐oxoacid dehydrogenase complex</subject><subject>3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide)</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Base Sequence</subject><subject>DNA Primers</subject><subject>electrostatic dipole vector</subject><subject>homology modeling</subject><subject>Ketone Oxidoreductases - metabolism</subject><subject>long‐range electrostatic interactions</subject><subject>Molecular Sequence Data</subject><subject>Multienzyme Complexes - metabolism</subject><subject>Mutagenesis, Site-Directed</subject><subject>Protein Binding</subject><subject>Protein Structure, Secondary</subject><subject>protein—protein recognition</subject><subject>Sequence Homology, Amino Acid</subject><subject>Static Electricity</subject><subject>structural analog</subject><subject>thioredoxin</subject><subject>Thioredoxins - chemistry</subject><subject>Thioredoxins - genetics</subject><subject>Thioredoxins - metabolism</subject><issn>0961-8368</issn><issn>1469-896X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kV1rFDEUhgdR7Fq98A9IbkVmm5PJZjJeCKX4UShUioJ3IZOc2U2ZmQxJxu7-Ov-aWadIRb1KTvKe5z0fRfES6BoA6NkU13INa7F5VKyAi6aUjfj2uFjRRkApKyFPimcx3lJKObDqaXEClAEFyVfFj8sxYdAmOT8S35G0cz6g9Xs3RnLn0o4kHbaYyBR8wvz4ltz4Ho_SSYfkzNzrQGIKs0lz0D3BHgccUyR6tMfApOBj0ll5REyYczD-5eTGHKML-ZLLmXp9WMxZ6fdeG2eJxd3BBr_FUUckxg9Tj3uMz4snne4jvrg_T4uvH95_ufhUXl1_vLw4vyoNB7Epta1aYeuaUQTaMsokp7StbcOgbjqomeDIWUVFwzqpG97VVFRGy6oDwyzF6rR4t3CnuR3Qmtxi7lZNwQ06HJTXTv35M7qd2vrvigHnADwDXi8Ak-cRA3a_c4Gq4xbVFJVUoMQma189NHugXNaWBWeL4M71ePg_SX2-uZYUfiHf3NvroQ3OblHd-jmMeWb_KOAn4KK9FQ</recordid><startdate>199901</startdate><enddate>199901</enddate><creator>BUNIK, VICTORIA</creator><creator>RADDATZ, GÜNTER</creator><creator>LEMAIRE, STEPHANE</creator><creator>MEYER, YVES</creator><creator>JACQUOT, JEAN-PIERRE</creator><creator>BISSWANGER, HANS</creator><general>Cambridge University Press</general><general>Cold Spring Harbor Laboratory Press</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>5PM</scope></search><sort><creationdate>199901</creationdate><title>Interaction of thioredoxins with target proteins: Role of particular structural elements and electrostatic properties of thioredoxins in their interplay with 2-oxoacid dehydrogenase complexes</title><author>BUNIK, VICTORIA ; RADDATZ, GÜNTER ; LEMAIRE, STEPHANE ; MEYER, YVES ; JACQUOT, JEAN-PIERRE ; BISSWANGER, HANS</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4165-ad3b6d7720e10b2028400b7d92179f17264e4230692f8a94f7063ca83f1c2d0e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1999</creationdate><topic>2‐oxoacid dehydrogenase complex</topic><topic>3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide)</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Base Sequence</topic><topic>DNA Primers</topic><topic>electrostatic dipole vector</topic><topic>homology modeling</topic><topic>Ketone Oxidoreductases - metabolism</topic><topic>long‐range electrostatic interactions</topic><topic>Molecular Sequence Data</topic><topic>Multienzyme Complexes - metabolism</topic><topic>Mutagenesis, Site-Directed</topic><topic>Protein Binding</topic><topic>Protein Structure, Secondary</topic><topic>protein—protein recognition</topic><topic>Sequence Homology, Amino Acid</topic><topic>Static Electricity</topic><topic>structural analog</topic><topic>thioredoxin</topic><topic>Thioredoxins - chemistry</topic><topic>Thioredoxins - genetics</topic><topic>Thioredoxins - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>BUNIK, VICTORIA</creatorcontrib><creatorcontrib>RADDATZ, GÜNTER</creatorcontrib><creatorcontrib>LEMAIRE, STEPHANE</creatorcontrib><creatorcontrib>MEYER, YVES</creatorcontrib><creatorcontrib>JACQUOT, JEAN-PIERRE</creatorcontrib><creatorcontrib>BISSWANGER, HANS</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Protein science</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>BUNIK, VICTORIA</au><au>RADDATZ, GÜNTER</au><au>LEMAIRE, STEPHANE</au><au>MEYER, YVES</au><au>JACQUOT, JEAN-PIERRE</au><au>BISSWANGER, HANS</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Interaction of thioredoxins with target proteins: Role of particular structural elements and electrostatic properties of thioredoxins in their interplay with 2-oxoacid dehydrogenase complexes</atitle><jtitle>Protein science</jtitle><addtitle>Protein Sci</addtitle><date>1999-01</date><risdate>1999</risdate><volume>8</volume><issue>1</issue><spage>65</spage><epage>74</epage><pages>65-74</pages><issn>0961-8368</issn><eissn>1469-896X</eissn><abstract>The thioredoxin action upon the 2-oxoacid dehydrogenase
complexes is investigated by using different thioredoxins,
both wild-type and mutated. The attacking cysteine residue
of thioredoxin is established to be essential for the thioredoxin-dependent
activation of the complexes. Mutation of the buried cysteine
residue to serine is not crucial for the activation, but
prevents inhibition of the complexes, exhibited by the
Clamydomonas reinhardtii thioredoxin m
disulfide. Site-directed mutagenesis of D26, W31, F/W12,
and Y/A70 (the Escherichia coli thioredoxin numbering
is employed for all the thioredoxins studied) indicates
that both the active site and remote residues of thioredoxin
are involved in its interplay with the 2-oxoacid dehydrogenase
complexes. Sequences of 11 thioredoxin species tested biochemically
are aligned. The thioredoxin residues at the contact between
the α3/310 and α1 helices, the length
of the α1 helix and the charges in the α2-β3
and β4-β5 linkers are found to correlate with the
protein influence on the 2-oxoacid dehydrogenase complexes
(the secondary structural elements of thioredoxin are defined
according to Eklund H et al., 1991, Proteins 11:13–28).
The distribution of the charges on the surface of the thioredoxin
molecules is analyzed. The analysis reveals the species
specific polarization of the thioredoxin active site surroundings,
which corresponds to the efficiency of the thioredoxin
interplay with the 2-oxoacid dehydrogenase systems. The
most effective mitochondrial thioredoxin is characterized
by the strongest polarization of this area and the highest
value of the electrostatic dipole vector of the molecule.
Not only the magnitude, but also the orientation of the
dipole vector show correlation with the thioredoxin action.
The dipole direction is found to be significantly influenced
by the charges of the residues 13/14, 51, and 83/85, which
distinguish the activating and inhibiting thioredoxin disulfides.</abstract><cop>Bristol</cop><pub>Cambridge University Press</pub><pmid>10210184</pmid><doi>10.1110/ps.8.1.65</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
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| ispartof | Protein science, 1999-01, Vol.8 (1), p.65-74 |
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| language | eng |
| recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_2144114 |
| source | MEDLINE; Wiley Online Library Journals Frontfile Complete; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Wiley Free Content; PubMed Central; Free Full-Text Journals in Chemistry |
| subjects | 2‐oxoacid dehydrogenase complex 3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide) Amino Acid Sequence Animals Base Sequence DNA Primers electrostatic dipole vector homology modeling Ketone Oxidoreductases - metabolism long‐range electrostatic interactions Molecular Sequence Data Multienzyme Complexes - metabolism Mutagenesis, Site-Directed Protein Binding Protein Structure, Secondary protein—protein recognition Sequence Homology, Amino Acid Static Electricity structural analog thioredoxin Thioredoxins - chemistry Thioredoxins - genetics Thioredoxins - metabolism |
| title | Interaction of thioredoxins with target proteins: Role of particular structural elements and electrostatic properties of thioredoxins in their interplay with 2-oxoacid dehydrogenase complexes |
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