Journal article 918 views
Functional and structural characterisation of a viral cytochromeb5
Emma L. Reid,
Karen D. Weynberg,
John Love,
Michail N. Isupov,
Jennifer A. Littlechild,
William H. Wilson,
Steven Kelly ,
David C. Lamb,
Michael J. Allen
FEBS Letters, Volume: 587, Issue: 22, Pages: 3633 - 3639
Swansea University Author: Steven Kelly
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DOI (Published version): 10.1016/j.febslet.2013.09.035
Abstract
Cytochrome b5 is a ubiquitous electron transport protein. The sequenced viral OtV-2 genome, which infects Ostreococcus tauri, was predicted to encode a putative cytochrome b5 enzyme. Using purified OtV-2 cytochrome b5 we confirm this protein has identical spectral properties to purified human cytoch...
Published in: | FEBS Letters |
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ISSN: | 0014-5793 |
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Wiley
2013
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URI: | https://cronfa.swan.ac.uk/Record/cronfa18159 |
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<?xml version="1.0"?><rfc1807><datestamp>2021-10-26T16:42:12.5462622</datestamp><bib-version>v2</bib-version><id>18159</id><entry>2014-07-24</entry><title>Functional and structural characterisation of a viral cytochromeb5</title><swanseaauthors><author><sid>b17cebaf09b4d737b9378a3581e3de93</sid><ORCID>0000-0001-7991-5040</ORCID><firstname>Steven</firstname><surname>Kelly</surname><name>Steven Kelly</name><active>true</active><ethesisStudent>false</ethesisStudent></author></swanseaauthors><date>2014-07-24</date><deptcode>BMS</deptcode><abstract>Cytochrome b5 is a ubiquitous electron transport protein. The sequenced viral OtV-2 genome, which infects Ostreococcus tauri, was predicted to encode a putative cytochrome b5 enzyme. Using purified OtV-2 cytochrome b5 we confirm this protein has identical spectral properties to purified human cytochrome b5 and additionally that the viral enzyme can substitute for yeast cytochrome b5 in yeast cytochrome P450 51 mediated sterol 14α-demethylation. The crystal structure of the OtV-2 cytochrome b5 enzyme reveals a single domain, comprising four β sheets, four α helices and a haem moiety, which is similar to that found in larger eukaryotic cytochrome proteins. As a product of a horizontal gene transfer event involving a subdomain of the host fumarate reductase-like protein, OtV-2 cytochrome b5 appears to have diverged in function and is likely to have evolved an entirely new role for the virus during infection. Indeed, lacking a hydrophobic C-terminal anchor, OtV-2 encodes the first cytosolic cytochrome b5 characterised. The lack of requirement for membrane attachment (in contrast to all other microsomal cytochrome b5s) may be a reflection of the small size of the host cell, further emphasizes the unique nature of this virus gene product and draws attention to the potential importance of cytochrome b5 metabolic activity at the extremes of cellular scale.</abstract><type>Journal Article</type><journal>FEBS Letters</journal><volume>587</volume><journalNumber>22</journalNumber><paginationStart>3633</paginationStart><paginationEnd>3639</paginationEnd><publisher>Wiley</publisher><placeOfPublication/><isbnPrint/><isbnElectronic/><issnPrint>0014-5793</issnPrint><issnElectronic/><keywords/><publishedDay>15</publishedDay><publishedMonth>11</publishedMonth><publishedYear>2013</publishedYear><publishedDate>2013-11-15</publishedDate><doi>10.1016/j.febslet.2013.09.035</doi><url>http://dx.doi.org/10.1016/j.febslet.2013.09.035</url><notes/><college>COLLEGE NANME</college><department>Biomedical Sciences</department><CollegeCode>COLLEGE CODE</CollegeCode><DepartmentCode>BMS</DepartmentCode><institution>Swansea University</institution><apcterm/><lastEdited>2021-10-26T16:42:12.5462622</lastEdited><Created>2014-07-24T14:37:10.0738663</Created><path><level id="1">Faculty of Medicine, Health and Life Sciences</level><level id="2">Swansea University Medical School - Medicine</level></path><authors><author><firstname>Emma L.</firstname><surname>Reid</surname><order>1</order></author><author><firstname>Karen D.</firstname><surname>Weynberg</surname><order>2</order></author><author><firstname>John</firstname><surname>Love</surname><order>3</order></author><author><firstname>Michail N.</firstname><surname>Isupov</surname><order>4</order></author><author><firstname>Jennifer A.</firstname><surname>Littlechild</surname><order>5</order></author><author><firstname>William H.</firstname><surname>Wilson</surname><order>6</order></author><author><firstname>Steven</firstname><surname>Kelly</surname><orcid>0000-0001-7991-5040</orcid><order>7</order></author><author><firstname>David C.</firstname><surname>Lamb</surname><order>8</order></author><author><firstname>Michael J.</firstname><surname>Allen</surname><order>9</order></author></authors><documents/><OutputDurs/></rfc1807> |
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2021-10-26T16:42:12.5462622 v2 18159 2014-07-24 Functional and structural characterisation of a viral cytochromeb5 b17cebaf09b4d737b9378a3581e3de93 0000-0001-7991-5040 Steven Kelly Steven Kelly true false 2014-07-24 BMS Cytochrome b5 is a ubiquitous electron transport protein. The sequenced viral OtV-2 genome, which infects Ostreococcus tauri, was predicted to encode a putative cytochrome b5 enzyme. Using purified OtV-2 cytochrome b5 we confirm this protein has identical spectral properties to purified human cytochrome b5 and additionally that the viral enzyme can substitute for yeast cytochrome b5 in yeast cytochrome P450 51 mediated sterol 14α-demethylation. The crystal structure of the OtV-2 cytochrome b5 enzyme reveals a single domain, comprising four β sheets, four α helices and a haem moiety, which is similar to that found in larger eukaryotic cytochrome proteins. As a product of a horizontal gene transfer event involving a subdomain of the host fumarate reductase-like protein, OtV-2 cytochrome b5 appears to have diverged in function and is likely to have evolved an entirely new role for the virus during infection. Indeed, lacking a hydrophobic C-terminal anchor, OtV-2 encodes the first cytosolic cytochrome b5 characterised. The lack of requirement for membrane attachment (in contrast to all other microsomal cytochrome b5s) may be a reflection of the small size of the host cell, further emphasizes the unique nature of this virus gene product and draws attention to the potential importance of cytochrome b5 metabolic activity at the extremes of cellular scale. Journal Article FEBS Letters 587 22 3633 3639 Wiley 0014-5793 15 11 2013 2013-11-15 10.1016/j.febslet.2013.09.035 http://dx.doi.org/10.1016/j.febslet.2013.09.035 COLLEGE NANME Biomedical Sciences COLLEGE CODE BMS Swansea University 2021-10-26T16:42:12.5462622 2014-07-24T14:37:10.0738663 Faculty of Medicine, Health and Life Sciences Swansea University Medical School - Medicine Emma L. Reid 1 Karen D. Weynberg 2 John Love 3 Michail N. Isupov 4 Jennifer A. Littlechild 5 William H. Wilson 6 Steven Kelly 0000-0001-7991-5040 7 David C. Lamb 8 Michael J. Allen 9 |
title |
Functional and structural characterisation of a viral cytochromeb5 |
spellingShingle |
Functional and structural characterisation of a viral cytochromeb5 Steven Kelly |
title_short |
Functional and structural characterisation of a viral cytochromeb5 |
title_full |
Functional and structural characterisation of a viral cytochromeb5 |
title_fullStr |
Functional and structural characterisation of a viral cytochromeb5 |
title_full_unstemmed |
Functional and structural characterisation of a viral cytochromeb5 |
title_sort |
Functional and structural characterisation of a viral cytochromeb5 |
author_id_str_mv |
b17cebaf09b4d737b9378a3581e3de93 |
author_id_fullname_str_mv |
b17cebaf09b4d737b9378a3581e3de93_***_Steven Kelly |
author |
Steven Kelly |
author2 |
Emma L. Reid Karen D. Weynberg John Love Michail N. Isupov Jennifer A. Littlechild William H. Wilson Steven Kelly David C. Lamb Michael J. Allen |
format |
Journal article |
container_title |
FEBS Letters |
container_volume |
587 |
container_issue |
22 |
container_start_page |
3633 |
publishDate |
2013 |
institution |
Swansea University |
issn |
0014-5793 |
doi_str_mv |
10.1016/j.febslet.2013.09.035 |
publisher |
Wiley |
college_str |
Faculty of Medicine, Health and Life Sciences |
hierarchytype |
|
hierarchy_top_id |
facultyofmedicinehealthandlifesciences |
hierarchy_top_title |
Faculty of Medicine, Health and Life Sciences |
hierarchy_parent_id |
facultyofmedicinehealthandlifesciences |
hierarchy_parent_title |
Faculty of Medicine, Health and Life Sciences |
department_str |
Swansea University Medical School - Medicine{{{_:::_}}}Faculty of Medicine, Health and Life Sciences{{{_:::_}}}Swansea University Medical School - Medicine |
url |
http://dx.doi.org/10.1016/j.febslet.2013.09.035 |
document_store_str |
0 |
active_str |
0 |
description |
Cytochrome b5 is a ubiquitous electron transport protein. The sequenced viral OtV-2 genome, which infects Ostreococcus tauri, was predicted to encode a putative cytochrome b5 enzyme. Using purified OtV-2 cytochrome b5 we confirm this protein has identical spectral properties to purified human cytochrome b5 and additionally that the viral enzyme can substitute for yeast cytochrome b5 in yeast cytochrome P450 51 mediated sterol 14α-demethylation. The crystal structure of the OtV-2 cytochrome b5 enzyme reveals a single domain, comprising four β sheets, four α helices and a haem moiety, which is similar to that found in larger eukaryotic cytochrome proteins. As a product of a horizontal gene transfer event involving a subdomain of the host fumarate reductase-like protein, OtV-2 cytochrome b5 appears to have diverged in function and is likely to have evolved an entirely new role for the virus during infection. Indeed, lacking a hydrophobic C-terminal anchor, OtV-2 encodes the first cytosolic cytochrome b5 characterised. The lack of requirement for membrane attachment (in contrast to all other microsomal cytochrome b5s) may be a reflection of the small size of the host cell, further emphasizes the unique nature of this virus gene product and draws attention to the potential importance of cytochrome b5 metabolic activity at the extremes of cellular scale. |
published_date |
2013-11-15T03:21:12Z |
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1763750626362130432 |
score |
11.016235 |