No Cover Image

Journal article 835 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 Orcid Logo, David C. Lamb, Michael J. Allen

FEBS Letters, Volume: 587, Issue: 22, Pages: 3633 - 3639

Swansea University Author: Steven Kelly Orcid Logo

Full text not available from this repository: check for access using links below.

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...

Full description

Published in: FEBS Letters
ISSN: 0014-5793
Published: Wiley 2013
Online Access: Check full text

URI: https://cronfa.swan.ac.uk/Record/cronfa18159
Tags: Add Tag
No Tags, Be the first to tag this record!
first_indexed 2014-07-25T01:30:22Z
last_indexed 2021-10-27T02:30:59Z
id cronfa18159
recordtype SURis
fullrecord <?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 14&#x3B1;-demethylation. The crystal structure of the OtV-2 cytochrome b5 enzyme reveals a single domain, comprising four &#x3B2; sheets, four &#x3B1; 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>
spelling 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
_version_ 1763750626362130432
score 10.998116