The respiratory chain complex thresholds in mitochondria of a Drosophila subobscura mutant strain
Analysis of a mutant strain of Drosophila subobscura revealed that most (80%) mitochondrial genomes have undergone a large scale deletion (5 kb) in the coding region. Compared with the wild-type strain, complex I and III activities are, respectively, reduced by 50% and 30% in the mutant. However, th...
Gespeichert in:
Veröffentlicht in: | Biochimie 2002-12, Vol.84 (12), p.1189-1197 |
---|---|
Hauptverfasser: | , , , |
Format: | Artikel |
Sprache: | eng |
Schlagworte: | |
Online-Zugang: | Volltext |
Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
container_end_page | 1197 |
---|---|
container_issue | 12 |
container_start_page | 1189 |
container_title | Biochimie |
container_volume | 84 |
creator | Farge, G. Touraille, S. Debise, R. Alziari, S. |
description | Analysis of a mutant strain of
Drosophila subobscura revealed that most (80%) mitochondrial genomes have undergone a large scale deletion (5 kb) in the coding region. Compared with the wild-type strain, complex I and III activities are, respectively, reduced by 50% and 30% in the mutant. However, the ATP synthesis capacities remain unchanged. In order to elucidate how the ATP synthesis is maintained at a normal level, despite a significant decrease in complex I and III activities, we progressively inhibited respiratory chain complex activities, respiration rate and ATP synthesis. Complex I, III and IV activities were inhibited by rotenone, antimycin and KCN, respectively. Threshold curves were thus determined for each complex. Our results demonstrated that in the mutant strain, both mitochondrial respiration and ATP synthesis had decreased when complex I activity was inhibited by more than 20%, whereas 70% inhibition is required to induce similar changes in the wild-type. The complex I inhibition pattern of the wild-type was restored by a backcross (mutant female/wild-type male). The complex III activity threshold is below 20% in both strains, and we observed some difference in antimycin sensitivity, suggesting a modification of the complex enzymatic properties in the mutant. In contrast, threshold values of 70% were measured for complex IV inhibition. Our data suggest that the difference in the complex I threshold curves between the wild-type and mutant strains could partially account for the absence of pathological phenotype in the mutant. |
doi_str_mv | 10.1016/S0300-9084(02)00038-X |
format | Article |
fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_19753691</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S030090840200038X</els_id><sourcerecordid>19753691</sourcerecordid><originalsourceid>FETCH-LOGICAL-c392t-59c391adf15ffbed760f58f7e04fe15ef1796294c7dbf250bd0fe04d39847a6d3</originalsourceid><addsrcrecordid>eNqFkE1v1DAQQC1ERZfCT6DyCcEh7dhZJ_GpqvoBSJU4tEi9WY49VlwlcWo7iP573O6qHDnNaObNjP0I-cTghAFrTm-hBqgkdNsvwL8CQN1V92_IhjUlaVhXvyWbV-SQvE_poUACuHxHDhlveMel2BB9NyCNmBYfdQ7xiZpB-5maMC0j_qF5KL0hjDbRUp18DmYIs41e0-CoppcxpLAMftQ0rX3ok1mjptOa9ZxpyrHs-kAOnB4TftzHI_Lr-uru4nt18_Pbj4vzm8rUkudKyBKZto4J53q0bQNOdK5F2DpkAh1rZcPl1rS2d1xAb8GVnq1lt211Y-sj8nm3d4nhccWU1eSTwXHUM4Y1KSZbUTeSFVDsQFMenyI6tUQ_6fikGKhnt-rFrXoWp4CrF7fqvswd7w-s_YT239ReZgHOdgCWb_72GFUyHmeD1kc0Wdng_3PiLyVci4Q</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>19753691</pqid></control><display><type>article</type><title>The respiratory chain complex thresholds in mitochondria of a Drosophila subobscura mutant strain</title><source>MEDLINE</source><source>ScienceDirect Journals (5 years ago - present)</source><creator>Farge, G. ; Touraille, S. ; Debise, R. ; Alziari, S.</creator><creatorcontrib>Farge, G. ; Touraille, S. ; Debise, R. ; Alziari, S.</creatorcontrib><description>Analysis of a mutant strain of
Drosophila subobscura revealed that most (80%) mitochondrial genomes have undergone a large scale deletion (5 kb) in the coding region. Compared with the wild-type strain, complex I and III activities are, respectively, reduced by 50% and 30% in the mutant. However, the ATP synthesis capacities remain unchanged. In order to elucidate how the ATP synthesis is maintained at a normal level, despite a significant decrease in complex I and III activities, we progressively inhibited respiratory chain complex activities, respiration rate and ATP synthesis. Complex I, III and IV activities were inhibited by rotenone, antimycin and KCN, respectively. Threshold curves were thus determined for each complex. Our results demonstrated that in the mutant strain, both mitochondrial respiration and ATP synthesis had decreased when complex I activity was inhibited by more than 20%, whereas 70% inhibition is required to induce similar changes in the wild-type. The complex I inhibition pattern of the wild-type was restored by a backcross (mutant female/wild-type male). The complex III activity threshold is below 20% in both strains, and we observed some difference in antimycin sensitivity, suggesting a modification of the complex enzymatic properties in the mutant. In contrast, threshold values of 70% were measured for complex IV inhibition. Our data suggest that the difference in the complex I threshold curves between the wild-type and mutant strains could partially account for the absence of pathological phenotype in the mutant.</description><identifier>ISSN: 0300-9084</identifier><identifier>EISSN: 1638-6183</identifier><identifier>DOI: 10.1016/S0300-9084(02)00038-X</identifier><identifier>PMID: 12628295</identifier><language>eng</language><publisher>France: Elsevier Masson SAS</publisher><subject>Adenosine Triphosphate - biosynthesis ; Animals ; Antimycin A - analogs & derivatives ; Antimycin A - pharmacology ; ATP synthesis ; Citrate (si)-Synthase - antagonists & inhibitors ; Citrate (si)-Synthase - metabolism ; Dose-Response Relationship, Drug ; Drosophila - genetics ; Drosophila - metabolism ; Drosophila subobscura ; Electron Transport - physiology ; Electron Transport Complex I - metabolism ; Electron Transport Complex III - antagonists & inhibitors ; Electron Transport Complex III - metabolism ; Electron Transport Complex IV - antagonists & inhibitors ; Electron Transport Complex IV - metabolism ; Enzyme Inhibitors - pharmacology ; Female ; Glycerophosphates - metabolism ; Heteroplasmy ; Kinetics ; Male ; Mitochondria - drug effects ; Mitochondria - enzymology ; Multienzyme Complexes - metabolism ; Mutation ; NADH, NADPH Oxidoreductases - antagonists & inhibitors ; NADH, NADPH Oxidoreductases - metabolism ; Oxidation-Reduction - drug effects ; Oxygen Consumption ; Potassium Cyanide - pharmacology ; Respiratory chain complexes ; Rotenone - pharmacology ; Threshold curves</subject><ispartof>Biochimie, 2002-12, Vol.84 (12), p.1189-1197</ispartof><rights>2003 Société française de biochimie et biologie moléculaire</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c392t-59c391adf15ffbed760f58f7e04fe15ef1796294c7dbf250bd0fe04d39847a6d3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/S0300-9084(02)00038-X$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3541,27915,27916,45986</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12628295$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Farge, G.</creatorcontrib><creatorcontrib>Touraille, S.</creatorcontrib><creatorcontrib>Debise, R.</creatorcontrib><creatorcontrib>Alziari, S.</creatorcontrib><title>The respiratory chain complex thresholds in mitochondria of a Drosophila subobscura mutant strain</title><title>Biochimie</title><addtitle>Biochimie</addtitle><description>Analysis of a mutant strain of
Drosophila subobscura revealed that most (80%) mitochondrial genomes have undergone a large scale deletion (5 kb) in the coding region. Compared with the wild-type strain, complex I and III activities are, respectively, reduced by 50% and 30% in the mutant. However, the ATP synthesis capacities remain unchanged. In order to elucidate how the ATP synthesis is maintained at a normal level, despite a significant decrease in complex I and III activities, we progressively inhibited respiratory chain complex activities, respiration rate and ATP synthesis. Complex I, III and IV activities were inhibited by rotenone, antimycin and KCN, respectively. Threshold curves were thus determined for each complex. Our results demonstrated that in the mutant strain, both mitochondrial respiration and ATP synthesis had decreased when complex I activity was inhibited by more than 20%, whereas 70% inhibition is required to induce similar changes in the wild-type. The complex I inhibition pattern of the wild-type was restored by a backcross (mutant female/wild-type male). The complex III activity threshold is below 20% in both strains, and we observed some difference in antimycin sensitivity, suggesting a modification of the complex enzymatic properties in the mutant. In contrast, threshold values of 70% were measured for complex IV inhibition. Our data suggest that the difference in the complex I threshold curves between the wild-type and mutant strains could partially account for the absence of pathological phenotype in the mutant.</description><subject>Adenosine Triphosphate - biosynthesis</subject><subject>Animals</subject><subject>Antimycin A - analogs & derivatives</subject><subject>Antimycin A - pharmacology</subject><subject>ATP synthesis</subject><subject>Citrate (si)-Synthase - antagonists & inhibitors</subject><subject>Citrate (si)-Synthase - metabolism</subject><subject>Dose-Response Relationship, Drug</subject><subject>Drosophila - genetics</subject><subject>Drosophila - metabolism</subject><subject>Drosophila subobscura</subject><subject>Electron Transport - physiology</subject><subject>Electron Transport Complex I - metabolism</subject><subject>Electron Transport Complex III - antagonists & inhibitors</subject><subject>Electron Transport Complex III - metabolism</subject><subject>Electron Transport Complex IV - antagonists & inhibitors</subject><subject>Electron Transport Complex IV - metabolism</subject><subject>Enzyme Inhibitors - pharmacology</subject><subject>Female</subject><subject>Glycerophosphates - metabolism</subject><subject>Heteroplasmy</subject><subject>Kinetics</subject><subject>Male</subject><subject>Mitochondria - drug effects</subject><subject>Mitochondria - enzymology</subject><subject>Multienzyme Complexes - metabolism</subject><subject>Mutation</subject><subject>NADH, NADPH Oxidoreductases - antagonists & inhibitors</subject><subject>NADH, NADPH Oxidoreductases - metabolism</subject><subject>Oxidation-Reduction - drug effects</subject><subject>Oxygen Consumption</subject><subject>Potassium Cyanide - pharmacology</subject><subject>Respiratory chain complexes</subject><subject>Rotenone - pharmacology</subject><subject>Threshold curves</subject><issn>0300-9084</issn><issn>1638-6183</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE1v1DAQQC1ERZfCT6DyCcEh7dhZJ_GpqvoBSJU4tEi9WY49VlwlcWo7iP573O6qHDnNaObNjP0I-cTghAFrTm-hBqgkdNsvwL8CQN1V92_IhjUlaVhXvyWbV-SQvE_poUACuHxHDhlveMel2BB9NyCNmBYfdQ7xiZpB-5maMC0j_qF5KL0hjDbRUp18DmYIs41e0-CoppcxpLAMftQ0rX3ok1mjptOa9ZxpyrHs-kAOnB4TftzHI_Lr-uru4nt18_Pbj4vzm8rUkudKyBKZto4J53q0bQNOdK5F2DpkAh1rZcPl1rS2d1xAb8GVnq1lt211Y-sj8nm3d4nhccWU1eSTwXHUM4Y1KSZbUTeSFVDsQFMenyI6tUQ_6fikGKhnt-rFrXoWp4CrF7fqvswd7w-s_YT239ReZgHOdgCWb_72GFUyHmeD1kc0Wdng_3PiLyVci4Q</recordid><startdate>20021201</startdate><enddate>20021201</enddate><creator>Farge, G.</creator><creator>Touraille, S.</creator><creator>Debise, R.</creator><creator>Alziari, S.</creator><general>Elsevier Masson SAS</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>7SS</scope></search><sort><creationdate>20021201</creationdate><title>The respiratory chain complex thresholds in mitochondria of a Drosophila subobscura mutant strain</title><author>Farge, G. ; Touraille, S. ; Debise, R. ; Alziari, S.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c392t-59c391adf15ffbed760f58f7e04fe15ef1796294c7dbf250bd0fe04d39847a6d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2002</creationdate><topic>Adenosine Triphosphate - biosynthesis</topic><topic>Animals</topic><topic>Antimycin A - analogs & derivatives</topic><topic>Antimycin A - pharmacology</topic><topic>ATP synthesis</topic><topic>Citrate (si)-Synthase - antagonists & inhibitors</topic><topic>Citrate (si)-Synthase - metabolism</topic><topic>Dose-Response Relationship, Drug</topic><topic>Drosophila - genetics</topic><topic>Drosophila - metabolism</topic><topic>Drosophila subobscura</topic><topic>Electron Transport - physiology</topic><topic>Electron Transport Complex I - metabolism</topic><topic>Electron Transport Complex III - antagonists & inhibitors</topic><topic>Electron Transport Complex III - metabolism</topic><topic>Electron Transport Complex IV - antagonists & inhibitors</topic><topic>Electron Transport Complex IV - metabolism</topic><topic>Enzyme Inhibitors - pharmacology</topic><topic>Female</topic><topic>Glycerophosphates - metabolism</topic><topic>Heteroplasmy</topic><topic>Kinetics</topic><topic>Male</topic><topic>Mitochondria - drug effects</topic><topic>Mitochondria - enzymology</topic><topic>Multienzyme Complexes - metabolism</topic><topic>Mutation</topic><topic>NADH, NADPH Oxidoreductases - antagonists & inhibitors</topic><topic>NADH, NADPH Oxidoreductases - metabolism</topic><topic>Oxidation-Reduction - drug effects</topic><topic>Oxygen Consumption</topic><topic>Potassium Cyanide - pharmacology</topic><topic>Respiratory chain complexes</topic><topic>Rotenone - pharmacology</topic><topic>Threshold curves</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Farge, G.</creatorcontrib><creatorcontrib>Touraille, S.</creatorcontrib><creatorcontrib>Debise, R.</creatorcontrib><creatorcontrib>Alziari, S.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Entomology Abstracts (Full archive)</collection><jtitle>Biochimie</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Farge, G.</au><au>Touraille, S.</au><au>Debise, R.</au><au>Alziari, S.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The respiratory chain complex thresholds in mitochondria of a Drosophila subobscura mutant strain</atitle><jtitle>Biochimie</jtitle><addtitle>Biochimie</addtitle><date>2002-12-01</date><risdate>2002</risdate><volume>84</volume><issue>12</issue><spage>1189</spage><epage>1197</epage><pages>1189-1197</pages><issn>0300-9084</issn><eissn>1638-6183</eissn><abstract>Analysis of a mutant strain of
Drosophila subobscura revealed that most (80%) mitochondrial genomes have undergone a large scale deletion (5 kb) in the coding region. Compared with the wild-type strain, complex I and III activities are, respectively, reduced by 50% and 30% in the mutant. However, the ATP synthesis capacities remain unchanged. In order to elucidate how the ATP synthesis is maintained at a normal level, despite a significant decrease in complex I and III activities, we progressively inhibited respiratory chain complex activities, respiration rate and ATP synthesis. Complex I, III and IV activities were inhibited by rotenone, antimycin and KCN, respectively. Threshold curves were thus determined for each complex. Our results demonstrated that in the mutant strain, both mitochondrial respiration and ATP synthesis had decreased when complex I activity was inhibited by more than 20%, whereas 70% inhibition is required to induce similar changes in the wild-type. The complex I inhibition pattern of the wild-type was restored by a backcross (mutant female/wild-type male). The complex III activity threshold is below 20% in both strains, and we observed some difference in antimycin sensitivity, suggesting a modification of the complex enzymatic properties in the mutant. In contrast, threshold values of 70% were measured for complex IV inhibition. Our data suggest that the difference in the complex I threshold curves between the wild-type and mutant strains could partially account for the absence of pathological phenotype in the mutant.</abstract><cop>France</cop><pub>Elsevier Masson SAS</pub><pmid>12628295</pmid><doi>10.1016/S0300-9084(02)00038-X</doi><tpages>9</tpages></addata></record> |
fulltext | fulltext |
identifier | ISSN: 0300-9084 |
ispartof | Biochimie, 2002-12, Vol.84 (12), p.1189-1197 |
issn | 0300-9084 1638-6183 |
language | eng |
recordid | cdi_proquest_miscellaneous_19753691 |
source | MEDLINE; ScienceDirect Journals (5 years ago - present) |
subjects | Adenosine Triphosphate - biosynthesis Animals Antimycin A - analogs & derivatives Antimycin A - pharmacology ATP synthesis Citrate (si)-Synthase - antagonists & inhibitors Citrate (si)-Synthase - metabolism Dose-Response Relationship, Drug Drosophila - genetics Drosophila - metabolism Drosophila subobscura Electron Transport - physiology Electron Transport Complex I - metabolism Electron Transport Complex III - antagonists & inhibitors Electron Transport Complex III - metabolism Electron Transport Complex IV - antagonists & inhibitors Electron Transport Complex IV - metabolism Enzyme Inhibitors - pharmacology Female Glycerophosphates - metabolism Heteroplasmy Kinetics Male Mitochondria - drug effects Mitochondria - enzymology Multienzyme Complexes - metabolism Mutation NADH, NADPH Oxidoreductases - antagonists & inhibitors NADH, NADPH Oxidoreductases - metabolism Oxidation-Reduction - drug effects Oxygen Consumption Potassium Cyanide - pharmacology Respiratory chain complexes Rotenone - pharmacology Threshold curves |
title | The respiratory chain complex thresholds in mitochondria of a Drosophila subobscura mutant strain |
url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-15T07%3A31%3A31IST&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=The%20respiratory%20chain%20complex%20thresholds%20in%20mitochondria%20of%20a%20Drosophila%20subobscura%20mutant%20strain&rft.jtitle=Biochimie&rft.au=Farge,%20G.&rft.date=2002-12-01&rft.volume=84&rft.issue=12&rft.spage=1189&rft.epage=1197&rft.pages=1189-1197&rft.issn=0300-9084&rft.eissn=1638-6183&rft_id=info:doi/10.1016/S0300-9084(02)00038-X&rft_dat=%3Cproquest_cross%3E19753691%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=19753691&rft_id=info:pmid/12628295&rft_els_id=S030090840200038X&rfr_iscdi=true |