Structure-function analysis of rgs1 in magnaporthe oryzae : role of DEP domains in subcellular targeting
Rgs1, a prototypical Regulator of G protein Signaling, negatively modulates the cyclic AMP pathway thereby influencing various aspects of asexual development and pathogenesis in the rice-blast fungus Magnaporthe oryzae. Rgs1 possesses tandem DEP motifs (termed DEP-A and DEP-B; for Dishevelled, Egl-1...
| Main Authors: | , , , |
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| Other Authors: | |
| Format: | Journal Article |
| Language: | English |
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2013
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| Online Access: | https://hdl.handle.net/10356/95053 http://hdl.handle.net/10220/9214 |
| _version_ | 1811678148527390720 |
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| author | Ramanujam, Ravikrishna. Yishi, Xu. Liu, Hao. Naqvi, Naweed Issak. |
| author2 | School of Biological Sciences |
| author_facet | School of Biological Sciences Ramanujam, Ravikrishna. Yishi, Xu. Liu, Hao. Naqvi, Naweed Issak. |
| author_sort | Ramanujam, Ravikrishna. |
| collection | NTU |
| description | Rgs1, a prototypical Regulator of G protein Signaling, negatively modulates the cyclic AMP pathway thereby influencing various aspects of asexual development and pathogenesis in the rice-blast fungus Magnaporthe oryzae. Rgs1 possesses tandem DEP motifs (termed DEP-A and DEP-B; for Dishevelled, Egl-10, Pleckstrin) at the N-terminus, and a Gα-GTP interacting RGS catalytic core domain at the C-terminus. In this study, we focused on gaining further insights into the mechanisms of Rgs1 regulation and subcellular localization by characterizing the role(s) of the individual domains and the full-length protein during asexual development and pathogenesis in Magnaporthe. Methodology/Principal Findings: Utilizing western blot analysis and specific antisera against the N- and C-terminal halves of Rgs1, we identify and report the in vivo endoproteolytic processing/cleavage of full-length Rgs1 that yields an N-terminal DEP and a RGS core domain. Independent expression of the resultant DEP-DEP half (N-Rgs1) or RGS core (C-Rgs1) fragments, failed to complement the rgs1Δ defects in colony morphology, aerial hyphal growth, surface hydrophobicity, conidiation, appressorium formation and infection. Interestingly, the full-length Rgs1-mCherry, as well as the tagged N-terminal DEP domains (individually or in conjunction) localized to distinct punctate vesicular structures in the cytosol, while the catalytic RGS core motif was predominantly vacuolar. |
| first_indexed | 2024-10-01T02:48:39Z |
| format | Journal Article |
| id | ntu-10356/95053 |
| institution | Nanyang Technological University |
| language | English |
| last_indexed | 2024-10-01T02:48:39Z |
| publishDate | 2013 |
| record_format | dspace |
| spelling | ntu-10356/950532023-02-28T16:56:19Z Structure-function analysis of rgs1 in magnaporthe oryzae : role of DEP domains in subcellular targeting Ramanujam, Ravikrishna. Yishi, Xu. Liu, Hao. Naqvi, Naweed Issak. School of Biological Sciences Rgs1, a prototypical Regulator of G protein Signaling, negatively modulates the cyclic AMP pathway thereby influencing various aspects of asexual development and pathogenesis in the rice-blast fungus Magnaporthe oryzae. Rgs1 possesses tandem DEP motifs (termed DEP-A and DEP-B; for Dishevelled, Egl-10, Pleckstrin) at the N-terminus, and a Gα-GTP interacting RGS catalytic core domain at the C-terminus. In this study, we focused on gaining further insights into the mechanisms of Rgs1 regulation and subcellular localization by characterizing the role(s) of the individual domains and the full-length protein during asexual development and pathogenesis in Magnaporthe. Methodology/Principal Findings: Utilizing western blot analysis and specific antisera against the N- and C-terminal halves of Rgs1, we identify and report the in vivo endoproteolytic processing/cleavage of full-length Rgs1 that yields an N-terminal DEP and a RGS core domain. Independent expression of the resultant DEP-DEP half (N-Rgs1) or RGS core (C-Rgs1) fragments, failed to complement the rgs1Δ defects in colony morphology, aerial hyphal growth, surface hydrophobicity, conidiation, appressorium formation and infection. Interestingly, the full-length Rgs1-mCherry, as well as the tagged N-terminal DEP domains (individually or in conjunction) localized to distinct punctate vesicular structures in the cytosol, while the catalytic RGS core motif was predominantly vacuolar. Published version 2013-02-21T07:03:21Z 2019-12-06T19:07:22Z 2013-02-21T07:03:21Z 2019-12-06T19:07:22Z 2012 2012 Journal Article Ramanujam, R., Yishi, X., Liu, H., & Naqvi, N. I. (2012). Structure-function analysis of rgs1 in magnaporthe oryzae : role of DEP domains in subcellular targeting. PLoS ONE, 7(7). 1932-6203 https://hdl.handle.net/10356/95053 http://hdl.handle.net/10220/9214 10.1371/journal.pone.0041084 22927898 en PLoS ONE © 2012 The Authors. application/pdf |
| spellingShingle | Ramanujam, Ravikrishna. Yishi, Xu. Liu, Hao. Naqvi, Naweed Issak. Structure-function analysis of rgs1 in magnaporthe oryzae : role of DEP domains in subcellular targeting |
| title | Structure-function analysis of rgs1 in magnaporthe oryzae : role of DEP domains in subcellular targeting |
| title_full | Structure-function analysis of rgs1 in magnaporthe oryzae : role of DEP domains in subcellular targeting |
| title_fullStr | Structure-function analysis of rgs1 in magnaporthe oryzae : role of DEP domains in subcellular targeting |
| title_full_unstemmed | Structure-function analysis of rgs1 in magnaporthe oryzae : role of DEP domains in subcellular targeting |
| title_short | Structure-function analysis of rgs1 in magnaporthe oryzae : role of DEP domains in subcellular targeting |
| title_sort | structure function analysis of rgs1 in magnaporthe oryzae role of dep domains in subcellular targeting |
| url | https://hdl.handle.net/10356/95053 http://hdl.handle.net/10220/9214 |
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