Evolution, three-dimensional model and localization of truncated hemoglobin PttTrHb of hybrid aspen.

Thus far, research on plant hemoglobins (Hbs) has mainly concentrated on symbiotic and non-symbiotic Hbs, and information on truncated Hbs (TrHbs) is scarce. The aim of this study was to examine the origin, structure and localization of the truncated Hb (PttTrHb) of hybrid aspen (Populus tremula L....

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Main Authors: Estelle Dumont, Soile Jokipii-Lukkari, Vimal Parkash, Jaana Vuosku, Robin Sundström, Yvonne Nymalm, Suvi Sutela, Katariina Taskinen, Pauli T Kallio, Tiina A Salminen, Hely Häggman
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2014-01-01
Series:PLoS ONE
Online Access:http://europepmc.org/articles/PMC3919811?pdf=render
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author Estelle Dumont
Soile Jokipii-Lukkari
Vimal Parkash
Jaana Vuosku
Robin Sundström
Yvonne Nymalm
Suvi Sutela
Katariina Taskinen
Pauli T Kallio
Tiina A Salminen
Hely Häggman
author_facet Estelle Dumont
Soile Jokipii-Lukkari
Vimal Parkash
Jaana Vuosku
Robin Sundström
Yvonne Nymalm
Suvi Sutela
Katariina Taskinen
Pauli T Kallio
Tiina A Salminen
Hely Häggman
author_sort Estelle Dumont
collection DOAJ
description Thus far, research on plant hemoglobins (Hbs) has mainly concentrated on symbiotic and non-symbiotic Hbs, and information on truncated Hbs (TrHbs) is scarce. The aim of this study was to examine the origin, structure and localization of the truncated Hb (PttTrHb) of hybrid aspen (Populus tremula L. × tremuloides Michx.), the model system of tree biology. Additionally, we studied the PttTrHb expression in relation to non-symbiotic class1 Hb gene (PttHb1) using RNAi-silenced hybrid aspen lines. Both the phylogenetic analysis and the three-dimensional (3D) model of PttTrHb supported the view that plant TrHbs evolved vertically from a bacterial TrHb. The 3D model suggested that PttTrHb adopts a 2-on-2 sandwich of α-helices and has a Bacillus subtilis -like ligand-binding pocket in which E11Gln and B10Tyr form hydrogen bonds to a ligand. However, due to differences in tunnel cavity and gate residue (E7Ala), it might not show similar ligand-binding kinetics as in Bs-HbO (E7Thr). The immunolocalization showed that PttTrHb protein was present in roots, stems as well as leaves of in vitro -grown hybrid aspens. In mature organs, PttTrHb was predominantly found in the vascular bundles and specifically at the site of lateral root formation, overlapping consistently with areas of nitric oxide (NO) production in plants. Furthermore, the NO donor sodium nitroprusside treatment increased the amount of PttTrHb in stems. The observed PttTrHb localization suggests that PttTrHb plays a role in the NO metabolism.
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spelling doaj.art-b1279006955f429bbc608b193c2db0f52022-12-21T19:29:33ZengPublic Library of Science (PLoS)PLoS ONE1932-62032014-01-0192e8857310.1371/journal.pone.0088573Evolution, three-dimensional model and localization of truncated hemoglobin PttTrHb of hybrid aspen.Estelle DumontSoile Jokipii-LukkariVimal ParkashJaana VuoskuRobin SundströmYvonne NymalmSuvi SutelaKatariina TaskinenPauli T KallioTiina A SalminenHely HäggmanThus far, research on plant hemoglobins (Hbs) has mainly concentrated on symbiotic and non-symbiotic Hbs, and information on truncated Hbs (TrHbs) is scarce. The aim of this study was to examine the origin, structure and localization of the truncated Hb (PttTrHb) of hybrid aspen (Populus tremula L. × tremuloides Michx.), the model system of tree biology. Additionally, we studied the PttTrHb expression in relation to non-symbiotic class1 Hb gene (PttHb1) using RNAi-silenced hybrid aspen lines. Both the phylogenetic analysis and the three-dimensional (3D) model of PttTrHb supported the view that plant TrHbs evolved vertically from a bacterial TrHb. The 3D model suggested that PttTrHb adopts a 2-on-2 sandwich of α-helices and has a Bacillus subtilis -like ligand-binding pocket in which E11Gln and B10Tyr form hydrogen bonds to a ligand. However, due to differences in tunnel cavity and gate residue (E7Ala), it might not show similar ligand-binding kinetics as in Bs-HbO (E7Thr). The immunolocalization showed that PttTrHb protein was present in roots, stems as well as leaves of in vitro -grown hybrid aspens. In mature organs, PttTrHb was predominantly found in the vascular bundles and specifically at the site of lateral root formation, overlapping consistently with areas of nitric oxide (NO) production in plants. Furthermore, the NO donor sodium nitroprusside treatment increased the amount of PttTrHb in stems. The observed PttTrHb localization suggests that PttTrHb plays a role in the NO metabolism.http://europepmc.org/articles/PMC3919811?pdf=render
spellingShingle Estelle Dumont
Soile Jokipii-Lukkari
Vimal Parkash
Jaana Vuosku
Robin Sundström
Yvonne Nymalm
Suvi Sutela
Katariina Taskinen
Pauli T Kallio
Tiina A Salminen
Hely Häggman
Evolution, three-dimensional model and localization of truncated hemoglobin PttTrHb of hybrid aspen.
PLoS ONE
title Evolution, three-dimensional model and localization of truncated hemoglobin PttTrHb of hybrid aspen.
title_full Evolution, three-dimensional model and localization of truncated hemoglobin PttTrHb of hybrid aspen.
title_fullStr Evolution, three-dimensional model and localization of truncated hemoglobin PttTrHb of hybrid aspen.
title_full_unstemmed Evolution, three-dimensional model and localization of truncated hemoglobin PttTrHb of hybrid aspen.
title_short Evolution, three-dimensional model and localization of truncated hemoglobin PttTrHb of hybrid aspen.
title_sort evolution three dimensional model and localization of truncated hemoglobin ptttrhb of hybrid aspen
url http://europepmc.org/articles/PMC3919811?pdf=render
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