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Ectromelia Virus Encodes a Novel Family of F-Box Proteins That Interact with the SCF Complex
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| Zeitschriftentitel: | Journal of Virology |
|---|---|
| Personen und Körperschaften: | , , , |
| In: | Journal of Virology, 82, 2008, 20, S. 9917-9927 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
American Society for Microbiology
|
| Schlagwörter: |
| author_facet |
van Buuren, Nick Couturier, Brianne Xiong, Yue Barry, Michele van Buuren, Nick Couturier, Brianne Xiong, Yue Barry, Michele |
|---|---|
| author |
van Buuren, Nick Couturier, Brianne Xiong, Yue Barry, Michele |
| spellingShingle |
van Buuren, Nick Couturier, Brianne Xiong, Yue Barry, Michele Journal of Virology Ectromelia Virus Encodes a Novel Family of F-Box Proteins That Interact with the SCF Complex Virology Insect Science Immunology Microbiology |
| author_sort |
van buuren, nick |
| spelling |
van Buuren, Nick Couturier, Brianne Xiong, Yue Barry, Michele 0022-538X 1098-5514 American Society for Microbiology Virology Insect Science Immunology Microbiology http://dx.doi.org/10.1128/jvi.00953-08 <jats:title>ABSTRACT</jats:title> <jats:p> Poxviruses are notorious for encoding multiple proteins that regulate cellular signaling pathways, including the ubiquitin-proteasome system. Bioinformatics indicated that ectromelia virus, the causative agent of lethal mousepox, encoded four proteins, EVM002, EVM005, EVM154, and EVM165, containing putative F-box domains. In contrast to cellular F-box proteins, the ectromelia virus proteins contain C-terminal F-box domains in conjunction with N-terminal ankyrin repeats, a combination that has not been previously reported for cellular proteins. These observations suggested that the ectromelia virus F-box proteins interact with SCF ( <jats:italic>S</jats:italic> kp1, <jats:italic>c</jats:italic> ullin-1, and <jats:italic>F</jats:italic> -box) ubiquitin ligases. We focused our studies on EVM005, since this protein had only one ortholog in cowpox virus. Using mass spectrometry, we identified cullin-1 as a binding partner for EVM005, and this interaction was confirmed by overexpression of hemagglutinin (HA)-cullin-1. During infection, Flag-EVM005 and HA-cullin-1 colocalized to distinct cellular bodies. Significantly, EVM005 coprecipitated with endogenous Skp1, cullin-1, and Roc1 and associated with conjugated ubiquitin, suggesting that EVM005 interacted with the components of a functional ubiquitin ligase. Interaction of EVM005 with cullin-1 and Skp1 was abolished upon deletion of the F-box, indicating that the F-box played a crucial role in interaction with the SCF complex. Additionally, EVM002 and EVM154 interacted with Skp1 and conjugated ubiquitin, suggesting that ectromelia virus encodes multiple F-box-containing proteins that regulate the SCF complex. Our results indicate that ectromelia virus has evolved multiple proteins that interact with the SCF complex. </jats:p> Ectromelia Virus Encodes a Novel Family of F-Box Proteins That Interact with the SCF Complex Journal of Virology |
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American Society for Microbiology, 2008 |
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American Society for Microbiology, 2008 |
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2008 |
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American Society for Microbiology |
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Journal of Virology |
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| title |
Ectromelia Virus Encodes a Novel Family of F-Box Proteins That Interact with the SCF Complex |
| title_unstemmed |
Ectromelia Virus Encodes a Novel Family of F-Box Proteins That Interact with the SCF Complex |
| title_full |
Ectromelia Virus Encodes a Novel Family of F-Box Proteins That Interact with the SCF Complex |
| title_fullStr |
Ectromelia Virus Encodes a Novel Family of F-Box Proteins That Interact with the SCF Complex |
| title_full_unstemmed |
Ectromelia Virus Encodes a Novel Family of F-Box Proteins That Interact with the SCF Complex |
| title_short |
Ectromelia Virus Encodes a Novel Family of F-Box Proteins That Interact with the SCF Complex |
| title_sort |
ectromelia virus encodes a novel family of f-box proteins that interact with the scf complex |
| topic |
Virology Insect Science Immunology Microbiology |
| url |
http://dx.doi.org/10.1128/jvi.00953-08 |
| publishDate |
2008 |
| physical |
9917-9927 |
| description |
<jats:title>ABSTRACT</jats:title>
<jats:p>
Poxviruses are notorious for encoding multiple proteins that regulate cellular signaling pathways, including the ubiquitin-proteasome system. Bioinformatics indicated that ectromelia virus, the causative agent of lethal mousepox, encoded four proteins, EVM002, EVM005, EVM154, and EVM165, containing putative F-box domains. In contrast to cellular F-box proteins, the ectromelia virus proteins contain C-terminal F-box domains in conjunction with N-terminal ankyrin repeats, a combination that has not been previously reported for cellular proteins. These observations suggested that the ectromelia virus F-box proteins interact with SCF (
<jats:italic>S</jats:italic>
kp1,
<jats:italic>c</jats:italic>
ullin-1, and
<jats:italic>F</jats:italic>
-box) ubiquitin ligases. We focused our studies on EVM005, since this protein had only one ortholog in cowpox virus. Using mass spectrometry, we identified cullin-1 as a binding partner for EVM005, and this interaction was confirmed by overexpression of hemagglutinin (HA)-cullin-1. During infection, Flag-EVM005 and HA-cullin-1 colocalized to distinct cellular bodies. Significantly, EVM005 coprecipitated with endogenous Skp1, cullin-1, and Roc1 and associated with conjugated ubiquitin, suggesting that EVM005 interacted with the components of a functional ubiquitin ligase. Interaction of EVM005 with cullin-1 and Skp1 was abolished upon deletion of the F-box, indicating that the F-box played a crucial role in interaction with the SCF complex. Additionally, EVM002 and EVM154 interacted with Skp1 and conjugated ubiquitin, suggesting that ectromelia virus encodes multiple F-box-containing proteins that regulate the SCF complex. Our results indicate that ectromelia virus has evolved multiple proteins that interact with the SCF complex.
</jats:p> |
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| author | van Buuren, Nick, Couturier, Brianne, Xiong, Yue, Barry, Michele |
| author_facet | van Buuren, Nick, Couturier, Brianne, Xiong, Yue, Barry, Michele, van Buuren, Nick, Couturier, Brianne, Xiong, Yue, Barry, Michele |
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| description | <jats:title>ABSTRACT</jats:title> <jats:p> Poxviruses are notorious for encoding multiple proteins that regulate cellular signaling pathways, including the ubiquitin-proteasome system. Bioinformatics indicated that ectromelia virus, the causative agent of lethal mousepox, encoded four proteins, EVM002, EVM005, EVM154, and EVM165, containing putative F-box domains. In contrast to cellular F-box proteins, the ectromelia virus proteins contain C-terminal F-box domains in conjunction with N-terminal ankyrin repeats, a combination that has not been previously reported for cellular proteins. These observations suggested that the ectromelia virus F-box proteins interact with SCF ( <jats:italic>S</jats:italic> kp1, <jats:italic>c</jats:italic> ullin-1, and <jats:italic>F</jats:italic> -box) ubiquitin ligases. We focused our studies on EVM005, since this protein had only one ortholog in cowpox virus. Using mass spectrometry, we identified cullin-1 as a binding partner for EVM005, and this interaction was confirmed by overexpression of hemagglutinin (HA)-cullin-1. During infection, Flag-EVM005 and HA-cullin-1 colocalized to distinct cellular bodies. Significantly, EVM005 coprecipitated with endogenous Skp1, cullin-1, and Roc1 and associated with conjugated ubiquitin, suggesting that EVM005 interacted with the components of a functional ubiquitin ligase. Interaction of EVM005 with cullin-1 and Skp1 was abolished upon deletion of the F-box, indicating that the F-box played a crucial role in interaction with the SCF complex. Additionally, EVM002 and EVM154 interacted with Skp1 and conjugated ubiquitin, suggesting that ectromelia virus encodes multiple F-box-containing proteins that regulate the SCF complex. Our results indicate that ectromelia virus has evolved multiple proteins that interact with the SCF complex. </jats:p> |
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| imprint | American Society for Microbiology, 2008 |
| imprint_str_mv | American Society for Microbiology, 2008 |
| institution | DE-D275, 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 |
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| spelling | van Buuren, Nick Couturier, Brianne Xiong, Yue Barry, Michele 0022-538X 1098-5514 American Society for Microbiology Virology Insect Science Immunology Microbiology http://dx.doi.org/10.1128/jvi.00953-08 <jats:title>ABSTRACT</jats:title> <jats:p> Poxviruses are notorious for encoding multiple proteins that regulate cellular signaling pathways, including the ubiquitin-proteasome system. Bioinformatics indicated that ectromelia virus, the causative agent of lethal mousepox, encoded four proteins, EVM002, EVM005, EVM154, and EVM165, containing putative F-box domains. In contrast to cellular F-box proteins, the ectromelia virus proteins contain C-terminal F-box domains in conjunction with N-terminal ankyrin repeats, a combination that has not been previously reported for cellular proteins. These observations suggested that the ectromelia virus F-box proteins interact with SCF ( <jats:italic>S</jats:italic> kp1, <jats:italic>c</jats:italic> ullin-1, and <jats:italic>F</jats:italic> -box) ubiquitin ligases. We focused our studies on EVM005, since this protein had only one ortholog in cowpox virus. Using mass spectrometry, we identified cullin-1 as a binding partner for EVM005, and this interaction was confirmed by overexpression of hemagglutinin (HA)-cullin-1. During infection, Flag-EVM005 and HA-cullin-1 colocalized to distinct cellular bodies. Significantly, EVM005 coprecipitated with endogenous Skp1, cullin-1, and Roc1 and associated with conjugated ubiquitin, suggesting that EVM005 interacted with the components of a functional ubiquitin ligase. Interaction of EVM005 with cullin-1 and Skp1 was abolished upon deletion of the F-box, indicating that the F-box played a crucial role in interaction with the SCF complex. Additionally, EVM002 and EVM154 interacted with Skp1 and conjugated ubiquitin, suggesting that ectromelia virus encodes multiple F-box-containing proteins that regulate the SCF complex. Our results indicate that ectromelia virus has evolved multiple proteins that interact with the SCF complex. </jats:p> Ectromelia Virus Encodes a Novel Family of F-Box Proteins That Interact with the SCF Complex Journal of Virology |
| spellingShingle | van Buuren, Nick, Couturier, Brianne, Xiong, Yue, Barry, Michele, Journal of Virology, Ectromelia Virus Encodes a Novel Family of F-Box Proteins That Interact with the SCF Complex, Virology, Insect Science, Immunology, Microbiology |
| title | Ectromelia Virus Encodes a Novel Family of F-Box Proteins That Interact with the SCF Complex |
| title_full | Ectromelia Virus Encodes a Novel Family of F-Box Proteins That Interact with the SCF Complex |
| title_fullStr | Ectromelia Virus Encodes a Novel Family of F-Box Proteins That Interact with the SCF Complex |
| title_full_unstemmed | Ectromelia Virus Encodes a Novel Family of F-Box Proteins That Interact with the SCF Complex |
| title_short | Ectromelia Virus Encodes a Novel Family of F-Box Proteins That Interact with the SCF Complex |
| title_sort | ectromelia virus encodes a novel family of f-box proteins that interact with the scf complex |
| title_unstemmed | Ectromelia Virus Encodes a Novel Family of F-Box Proteins That Interact with the SCF Complex |
| topic | Virology, Insect Science, Immunology, Microbiology |
| url | http://dx.doi.org/10.1128/jvi.00953-08 |