Eintrag weiter verarbeiten
The F1‐ATPase from Trypanosoma brucei is elaborated by three copies of an additional p18‐subunit
Gespeichert in:
| Zeitschriftentitel: | The FEBS Journal |
|---|---|
| Personen und Körperschaften: | , , , , , , , |
| In: | The FEBS Journal, 285, 2018, 3, S. 614-628 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Wiley
|
| Schlagwörter: |
| author_facet |
Gahura, Ondřej Šubrtová, Karolína Váchová, Hana Panicucci, Brian Fearnley, Ian M. Harbour, Michael E. Walker, John E. Zíková, Alena Gahura, Ondřej Šubrtová, Karolína Váchová, Hana Panicucci, Brian Fearnley, Ian M. Harbour, Michael E. Walker, John E. Zíková, Alena |
|---|---|
| author |
Gahura, Ondřej Šubrtová, Karolína Váchová, Hana Panicucci, Brian Fearnley, Ian M. Harbour, Michael E. Walker, John E. Zíková, Alena |
| spellingShingle |
Gahura, Ondřej Šubrtová, Karolína Váchová, Hana Panicucci, Brian Fearnley, Ian M. Harbour, Michael E. Walker, John E. Zíková, Alena The FEBS Journal The F1‐ATPase from Trypanosoma brucei is elaborated by three copies of an additional p18‐subunit Cell Biology Molecular Biology Biochemistry |
| author_sort |
gahura, ondřej |
| spelling |
Gahura, Ondřej Šubrtová, Karolína Váchová, Hana Panicucci, Brian Fearnley, Ian M. Harbour, Michael E. Walker, John E. Zíková, Alena 1742-464X 1742-4658 Wiley Cell Biology Molecular Biology Biochemistry http://dx.doi.org/10.1111/febs.14364 <jats:p>The F‐<jats:styled-content style="fixed-case">ATP</jats:styled-content>ases (also called the F<jats:sub>1</jats:sub>F<jats:sub>o</jats:sub>‐<jats:styled-content style="fixed-case">ATP</jats:styled-content>ases or <jats:styled-content style="fixed-case">ATP</jats:styled-content> synthases) are multi‐subunit membrane‐bound molecular machines that produce <jats:styled-content style="fixed-case">ATP</jats:styled-content> in bacteria and in eukaryotic mitochondria and chloroplasts. The structures and enzymic mechanisms of their F<jats:sub>1</jats:sub>‐catalytic domains are highly conserved in all species investigated hitherto. However, there is evidence that the F‐<jats:styled-content style="fixed-case">ATP</jats:styled-content>ases from the group of protozoa known as Euglenozoa have novel features. Therefore, we have isolated pure and active F<jats:sub>1</jats:sub>‐<jats:styled-content style="fixed-case">ATP</jats:styled-content>ase from the euglenozoan parasite, <jats:italic>Trypanosoma brucei</jats:italic>, and characterized it. All of the usual eukaryotic subunits (α, β, γ, δ, and ε) were present in the enzyme, and, in addition, two unique features were detected. First, each of the three α‐subunits in the F<jats:sub>1</jats:sub>‐domain has been cleaved by proteolysis <jats:italic>in vivo</jats:italic> at two sites eight residues apart, producing two assembled fragments. Second, the <jats:italic>T. brucei</jats:italic> F<jats:sub>1</jats:sub>‐<jats:styled-content style="fixed-case">ATP</jats:styled-content>ase has an additional subunit, called p18, present in three copies per complex. Suppression of expression of p18 affected <jats:italic>in vitro</jats:italic> growth of both the insect and infectious mammalian forms of <jats:italic>T. brucei</jats:italic>. It also reduced the levels of monomeric and multimeric F‐<jats:styled-content style="fixed-case">ATP</jats:styled-content>ase complexes and diminished the <jats:italic>in vivo</jats:italic> hydrolytic activity of the enzyme significantly. These observations imply that p18 plays a role in the assembly of the F<jats:sub>1</jats:sub> domain. These unique features of the F<jats:sub>1</jats:sub>‐<jats:styled-content style="fixed-case">ATP</jats:styled-content>ase extend the list of special characteristics of the F‐<jats:styled-content style="fixed-case">ATP</jats:styled-content>ase from <jats:italic>T. brucei</jats:italic>, and also, demonstrate that the architecture of the F<jats:sub>1</jats:sub>‐<jats:styled-content style="fixed-case">ATP</jats:styled-content>ase complex is not strictly conserved in eukaryotes.</jats:p> The F<sub>1</sub>‐<scp>ATP</scp>ase from <i>Trypanosoma brucei</i> is elaborated by three copies of an additional p18‐subunit The FEBS Journal |
| doi_str_mv |
10.1111/febs.14364 |
| facet_avail |
Online Free |
| finc_class_facet |
Biologie Chemie und Pharmazie |
| format |
ElectronicArticle |
| fullrecord |
blob:ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTExMS9mZWJzLjE0MzY0 |
| id |
ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTExMS9mZWJzLjE0MzY0 |
| institution |
DE-Bn3 DE-Brt1 DE-Zwi2 DE-D161 DE-Gla1 DE-Zi4 DE-15 DE-Pl11 DE-Rs1 DE-105 DE-14 DE-Ch1 DE-L229 DE-D275 |
| imprint |
Wiley, 2018 |
| imprint_str_mv |
Wiley, 2018 |
| issn |
1742-464X 1742-4658 |
| issn_str_mv |
1742-464X 1742-4658 |
| language |
English |
| mega_collection |
Wiley (CrossRef) |
| match_str |
gahura2018thef1atpasefromtrypanosomabruceiiselaboratedbythreecopiesofanadditionalp18subunit |
| publishDateSort |
2018 |
| publisher |
Wiley |
| recordtype |
ai |
| record_format |
ai |
| series |
The FEBS Journal |
| source_id |
49 |
| title |
The F1‐ATPase from Trypanosoma brucei is elaborated by three copies of an additional p18‐subunit |
| title_unstemmed |
The F1‐ATPase from Trypanosoma brucei is elaborated by three copies of an additional p18‐subunit |
| title_full |
The F1‐ATPase from Trypanosoma brucei is elaborated by three copies of an additional p18‐subunit |
| title_fullStr |
The F1‐ATPase from Trypanosoma brucei is elaborated by three copies of an additional p18‐subunit |
| title_full_unstemmed |
The F1‐ATPase from Trypanosoma brucei is elaborated by three copies of an additional p18‐subunit |
| title_short |
The F1‐ATPase from Trypanosoma brucei is elaborated by three copies of an additional p18‐subunit |
| title_sort |
the f<sub>1</sub>‐<scp>atp</scp>ase from <i>trypanosoma brucei</i> is elaborated by three copies of an additional p18‐subunit |
| topic |
Cell Biology Molecular Biology Biochemistry |
| url |
http://dx.doi.org/10.1111/febs.14364 |
| publishDate |
2018 |
| physical |
614-628 |
| description |
<jats:p>The F‐<jats:styled-content style="fixed-case">ATP</jats:styled-content>ases (also called the F<jats:sub>1</jats:sub>F<jats:sub>o</jats:sub>‐<jats:styled-content style="fixed-case">ATP</jats:styled-content>ases or <jats:styled-content style="fixed-case">ATP</jats:styled-content> synthases) are multi‐subunit membrane‐bound molecular machines that produce <jats:styled-content style="fixed-case">ATP</jats:styled-content> in bacteria and in eukaryotic mitochondria and chloroplasts. The structures and enzymic mechanisms of their F<jats:sub>1</jats:sub>‐catalytic domains are highly conserved in all species investigated hitherto. However, there is evidence that the F‐<jats:styled-content style="fixed-case">ATP</jats:styled-content>ases from the group of protozoa known as Euglenozoa have novel features. Therefore, we have isolated pure and active F<jats:sub>1</jats:sub>‐<jats:styled-content style="fixed-case">ATP</jats:styled-content>ase from the euglenozoan parasite, <jats:italic>Trypanosoma brucei</jats:italic>, and characterized it. All of the usual eukaryotic subunits (α, β, γ, δ, and ε) were present in the enzyme, and, in addition, two unique features were detected. First, each of the three α‐subunits in the F<jats:sub>1</jats:sub>‐domain has been cleaved by proteolysis <jats:italic>in vivo</jats:italic> at two sites eight residues apart, producing two assembled fragments. Second, the <jats:italic>T. brucei</jats:italic> F<jats:sub>1</jats:sub>‐<jats:styled-content style="fixed-case">ATP</jats:styled-content>ase has an additional subunit, called p18, present in three copies per complex. Suppression of expression of p18 affected <jats:italic>in vitro</jats:italic> growth of both the insect and infectious mammalian forms of <jats:italic>T. brucei</jats:italic>. It also reduced the levels of monomeric and multimeric F‐<jats:styled-content style="fixed-case">ATP</jats:styled-content>ase complexes and diminished the <jats:italic>in vivo</jats:italic> hydrolytic activity of the enzyme significantly. These observations imply that p18 plays a role in the assembly of the F<jats:sub>1</jats:sub> domain. These unique features of the F<jats:sub>1</jats:sub>‐<jats:styled-content style="fixed-case">ATP</jats:styled-content>ase extend the list of special characteristics of the F‐<jats:styled-content style="fixed-case">ATP</jats:styled-content>ase from <jats:italic>T. brucei</jats:italic>, and also, demonstrate that the architecture of the F<jats:sub>1</jats:sub>‐<jats:styled-content style="fixed-case">ATP</jats:styled-content>ase complex is not strictly conserved in eukaryotes.</jats:p> |
| container_issue |
3 |
| container_start_page |
614 |
| container_title |
The FEBS Journal |
| container_volume |
285 |
| format_de105 |
Article, E-Article |
| format_de14 |
Article, E-Article |
| format_de15 |
Article, E-Article |
| format_de520 |
Article, E-Article |
| format_de540 |
Article, E-Article |
| format_dech1 |
Article, E-Article |
| format_ded117 |
Article, E-Article |
| format_degla1 |
E-Article |
| format_del152 |
Buch |
| format_del189 |
Article, E-Article |
| format_dezi4 |
Article |
| format_dezwi2 |
Article, E-Article |
| format_finc |
Article, E-Article |
| format_nrw |
Article, E-Article |
| _version_ |
1792337693800136705 |
| geogr_code |
not assigned |
| last_indexed |
2024-03-01T15:19:56.517Z |
| geogr_code_person |
not assigned |
| openURL |
url_ver=Z39.88-2004&ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fvufind.svn.sourceforge.net%3Agenerator&rft.title=The+F1%E2%80%90ATPase+from+Trypanosoma+brucei+is+elaborated+by+three+copies+of+an+additional+p18%E2%80%90subunit&rft.date=2018-02-01&genre=article&issn=1742-4658&volume=285&issue=3&spage=614&epage=628&pages=614-628&jtitle=The+FEBS+Journal&atitle=The+F%3Csub%3E1%3C%2Fsub%3E%E2%80%90%3Cscp%3EATP%3C%2Fscp%3Ease+from+%3Ci%3ETrypanosoma+brucei%3C%2Fi%3E+is+elaborated+by+three+copies+of+an+additional+p18%E2%80%90subunit&aulast=Z%C3%ADkov%C3%A1&aufirst=Alena&rft_id=info%3Adoi%2F10.1111%2Ffebs.14364&rft.language%5B0%5D=eng |
| SOLR | |
| _version_ | 1792337693800136705 |
| author | Gahura, Ondřej, Šubrtová, Karolína, Váchová, Hana, Panicucci, Brian, Fearnley, Ian M., Harbour, Michael E., Walker, John E., Zíková, Alena |
| author_facet | Gahura, Ondřej, Šubrtová, Karolína, Váchová, Hana, Panicucci, Brian, Fearnley, Ian M., Harbour, Michael E., Walker, John E., Zíková, Alena, Gahura, Ondřej, Šubrtová, Karolína, Váchová, Hana, Panicucci, Brian, Fearnley, Ian M., Harbour, Michael E., Walker, John E., Zíková, Alena |
| author_sort | gahura, ondřej |
| container_issue | 3 |
| container_start_page | 614 |
| container_title | The FEBS Journal |
| container_volume | 285 |
| description | <jats:p>The F‐<jats:styled-content style="fixed-case">ATP</jats:styled-content>ases (also called the F<jats:sub>1</jats:sub>F<jats:sub>o</jats:sub>‐<jats:styled-content style="fixed-case">ATP</jats:styled-content>ases or <jats:styled-content style="fixed-case">ATP</jats:styled-content> synthases) are multi‐subunit membrane‐bound molecular machines that produce <jats:styled-content style="fixed-case">ATP</jats:styled-content> in bacteria and in eukaryotic mitochondria and chloroplasts. The structures and enzymic mechanisms of their F<jats:sub>1</jats:sub>‐catalytic domains are highly conserved in all species investigated hitherto. However, there is evidence that the F‐<jats:styled-content style="fixed-case">ATP</jats:styled-content>ases from the group of protozoa known as Euglenozoa have novel features. Therefore, we have isolated pure and active F<jats:sub>1</jats:sub>‐<jats:styled-content style="fixed-case">ATP</jats:styled-content>ase from the euglenozoan parasite, <jats:italic>Trypanosoma brucei</jats:italic>, and characterized it. All of the usual eukaryotic subunits (α, β, γ, δ, and ε) were present in the enzyme, and, in addition, two unique features were detected. First, each of the three α‐subunits in the F<jats:sub>1</jats:sub>‐domain has been cleaved by proteolysis <jats:italic>in vivo</jats:italic> at two sites eight residues apart, producing two assembled fragments. Second, the <jats:italic>T. brucei</jats:italic> F<jats:sub>1</jats:sub>‐<jats:styled-content style="fixed-case">ATP</jats:styled-content>ase has an additional subunit, called p18, present in three copies per complex. Suppression of expression of p18 affected <jats:italic>in vitro</jats:italic> growth of both the insect and infectious mammalian forms of <jats:italic>T. brucei</jats:italic>. It also reduced the levels of monomeric and multimeric F‐<jats:styled-content style="fixed-case">ATP</jats:styled-content>ase complexes and diminished the <jats:italic>in vivo</jats:italic> hydrolytic activity of the enzyme significantly. These observations imply that p18 plays a role in the assembly of the F<jats:sub>1</jats:sub> domain. These unique features of the F<jats:sub>1</jats:sub>‐<jats:styled-content style="fixed-case">ATP</jats:styled-content>ase extend the list of special characteristics of the F‐<jats:styled-content style="fixed-case">ATP</jats:styled-content>ase from <jats:italic>T. brucei</jats:italic>, and also, demonstrate that the architecture of the F<jats:sub>1</jats:sub>‐<jats:styled-content style="fixed-case">ATP</jats:styled-content>ase complex is not strictly conserved in eukaryotes.</jats:p> |
| doi_str_mv | 10.1111/febs.14364 |
| facet_avail | Online, Free |
| finc_class_facet | Biologie, Chemie und Pharmazie |
| format | ElectronicArticle |
| format_de105 | Article, E-Article |
| format_de14 | Article, E-Article |
| format_de15 | Article, E-Article |
| format_de520 | Article, E-Article |
| format_de540 | Article, E-Article |
| format_dech1 | Article, E-Article |
| format_ded117 | Article, E-Article |
| format_degla1 | E-Article |
| format_del152 | Buch |
| format_del189 | Article, E-Article |
| format_dezi4 | Article |
| format_dezwi2 | Article, E-Article |
| format_finc | Article, E-Article |
| format_nrw | Article, E-Article |
| geogr_code | not assigned |
| geogr_code_person | not assigned |
| id | ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTExMS9mZWJzLjE0MzY0 |
| imprint | Wiley, 2018 |
| imprint_str_mv | Wiley, 2018 |
| institution | DE-Bn3, DE-Brt1, DE-Zwi2, DE-D161, DE-Gla1, DE-Zi4, DE-15, DE-Pl11, DE-Rs1, DE-105, DE-14, DE-Ch1, DE-L229, DE-D275 |
| issn | 1742-464X, 1742-4658 |
| issn_str_mv | 1742-464X, 1742-4658 |
| language | English |
| last_indexed | 2024-03-01T15:19:56.517Z |
| match_str | gahura2018thef1atpasefromtrypanosomabruceiiselaboratedbythreecopiesofanadditionalp18subunit |
| mega_collection | Wiley (CrossRef) |
| physical | 614-628 |
| publishDate | 2018 |
| publishDateSort | 2018 |
| publisher | Wiley |
| record_format | ai |
| recordtype | ai |
| series | The FEBS Journal |
| source_id | 49 |
| spelling | Gahura, Ondřej Šubrtová, Karolína Váchová, Hana Panicucci, Brian Fearnley, Ian M. Harbour, Michael E. Walker, John E. Zíková, Alena 1742-464X 1742-4658 Wiley Cell Biology Molecular Biology Biochemistry http://dx.doi.org/10.1111/febs.14364 <jats:p>The F‐<jats:styled-content style="fixed-case">ATP</jats:styled-content>ases (also called the F<jats:sub>1</jats:sub>F<jats:sub>o</jats:sub>‐<jats:styled-content style="fixed-case">ATP</jats:styled-content>ases or <jats:styled-content style="fixed-case">ATP</jats:styled-content> synthases) are multi‐subunit membrane‐bound molecular machines that produce <jats:styled-content style="fixed-case">ATP</jats:styled-content> in bacteria and in eukaryotic mitochondria and chloroplasts. The structures and enzymic mechanisms of their F<jats:sub>1</jats:sub>‐catalytic domains are highly conserved in all species investigated hitherto. However, there is evidence that the F‐<jats:styled-content style="fixed-case">ATP</jats:styled-content>ases from the group of protozoa known as Euglenozoa have novel features. Therefore, we have isolated pure and active F<jats:sub>1</jats:sub>‐<jats:styled-content style="fixed-case">ATP</jats:styled-content>ase from the euglenozoan parasite, <jats:italic>Trypanosoma brucei</jats:italic>, and characterized it. All of the usual eukaryotic subunits (α, β, γ, δ, and ε) were present in the enzyme, and, in addition, two unique features were detected. First, each of the three α‐subunits in the F<jats:sub>1</jats:sub>‐domain has been cleaved by proteolysis <jats:italic>in vivo</jats:italic> at two sites eight residues apart, producing two assembled fragments. Second, the <jats:italic>T. brucei</jats:italic> F<jats:sub>1</jats:sub>‐<jats:styled-content style="fixed-case">ATP</jats:styled-content>ase has an additional subunit, called p18, present in three copies per complex. Suppression of expression of p18 affected <jats:italic>in vitro</jats:italic> growth of both the insect and infectious mammalian forms of <jats:italic>T. brucei</jats:italic>. It also reduced the levels of monomeric and multimeric F‐<jats:styled-content style="fixed-case">ATP</jats:styled-content>ase complexes and diminished the <jats:italic>in vivo</jats:italic> hydrolytic activity of the enzyme significantly. These observations imply that p18 plays a role in the assembly of the F<jats:sub>1</jats:sub> domain. These unique features of the F<jats:sub>1</jats:sub>‐<jats:styled-content style="fixed-case">ATP</jats:styled-content>ase extend the list of special characteristics of the F‐<jats:styled-content style="fixed-case">ATP</jats:styled-content>ase from <jats:italic>T. brucei</jats:italic>, and also, demonstrate that the architecture of the F<jats:sub>1</jats:sub>‐<jats:styled-content style="fixed-case">ATP</jats:styled-content>ase complex is not strictly conserved in eukaryotes.</jats:p> The F<sub>1</sub>‐<scp>ATP</scp>ase from <i>Trypanosoma brucei</i> is elaborated by three copies of an additional p18‐subunit The FEBS Journal |
| spellingShingle | Gahura, Ondřej, Šubrtová, Karolína, Váchová, Hana, Panicucci, Brian, Fearnley, Ian M., Harbour, Michael E., Walker, John E., Zíková, Alena, The FEBS Journal, The F1‐ATPase from Trypanosoma brucei is elaborated by three copies of an additional p18‐subunit, Cell Biology, Molecular Biology, Biochemistry |
| title | The F1‐ATPase from Trypanosoma brucei is elaborated by three copies of an additional p18‐subunit |
| title_full | The F1‐ATPase from Trypanosoma brucei is elaborated by three copies of an additional p18‐subunit |
| title_fullStr | The F1‐ATPase from Trypanosoma brucei is elaborated by three copies of an additional p18‐subunit |
| title_full_unstemmed | The F1‐ATPase from Trypanosoma brucei is elaborated by three copies of an additional p18‐subunit |
| title_short | The F1‐ATPase from Trypanosoma brucei is elaborated by three copies of an additional p18‐subunit |
| title_sort | the f<sub>1</sub>‐<scp>atp</scp>ase from <i>trypanosoma brucei</i> is elaborated by three copies of an additional p18‐subunit |
| title_unstemmed | The F1‐ATPase from Trypanosoma brucei is elaborated by three copies of an additional p18‐subunit |
| topic | Cell Biology, Molecular Biology, Biochemistry |
| url | http://dx.doi.org/10.1111/febs.14364 |