Serine hydroxymethyltransferase localised in the endoplasmic reticulum plays a role in scavenging H2O2 to enhance rice chilling tolerance
Background: Rice is a chilling-sensitive crop that would suffer serious damage from low temperatures. Overexpression of the Lsi1 gene (Lsi1-OX) in rice enhances its chilling tolerance. This study revealed that a serine hydroxymethyltransferase (OsSHMT) mainly localised in the endoplasmic reticulum (ER) is involved in increasing tolerance to chilling.
Results: A higher transcription level of OsSHMT was detected in Lsi1-OX rice than in the wild type. Histone H1 and nucleic acid binding protein were found to bind to the promoter region of OsSHMT and regulate its expression, and the transcription levels of these proteins were also up-regulated in the Lsi1-OX rice. Moreover, OsSHMT interacts with ATP synthase subunit α, heat shock protein Hsp70, mitochondrial substrate carrier family protein, ascorbate peroxidase 1 and ATP synthase subunit β. Lsi1-encoded protein OsNIP2;1 also interacts with ATP synthase subunit β, and the coordination of these proteins appears to function in reducing reactive oxygen species, as the H2O2 content of transgenic OsSHMT Arabidopsis thaliana was lower than that of the non-transgenic line under chilling treatment.
Conclusions: Our results indicate that ER-localised OsSHMT plays a role in scavenging H2O2 to enhance the chilling tolerance of Lsi1-OX rice and that ATP synthase subunit β is an intermediate junction between OsNIP2;1 and OsSHMT.
Figure 1
Figure 2
Figure 3
Figure 4
Figure 5
Figure 6
Figure 7
Figure 8
This is a list of supplementary files associated with this preprint. Click to download.
Posted 19 May, 2020
On 06 May, 2020
On 05 May, 2020
On 18 Feb, 2020
On 05 May, 2020
Received 22 Apr, 2020
On 31 Mar, 2020
Received 28 Mar, 2020
Invitations sent on 28 Mar, 2020
On 28 Mar, 2020
On 25 Mar, 2020
On 24 Mar, 2020
On 24 Mar, 2020
On 13 Mar, 2020
Received 12 Mar, 2020
Received 05 Mar, 2020
On 28 Feb, 2020
On 27 Feb, 2020
Invitations sent on 27 Feb, 2020
On 27 Feb, 2020
On 19 Feb, 2020
On 19 Feb, 2020
Serine hydroxymethyltransferase localised in the endoplasmic reticulum plays a role in scavenging H2O2 to enhance rice chilling tolerance
Posted 19 May, 2020
On 06 May, 2020
On 05 May, 2020
On 18 Feb, 2020
On 05 May, 2020
Received 22 Apr, 2020
On 31 Mar, 2020
Received 28 Mar, 2020
Invitations sent on 28 Mar, 2020
On 28 Mar, 2020
On 25 Mar, 2020
On 24 Mar, 2020
On 24 Mar, 2020
On 13 Mar, 2020
Received 12 Mar, 2020
Received 05 Mar, 2020
On 28 Feb, 2020
On 27 Feb, 2020
Invitations sent on 27 Feb, 2020
On 27 Feb, 2020
On 19 Feb, 2020
On 19 Feb, 2020
Background: Rice is a chilling-sensitive crop that would suffer serious damage from low temperatures. Overexpression of the Lsi1 gene (Lsi1-OX) in rice enhances its chilling tolerance. This study revealed that a serine hydroxymethyltransferase (OsSHMT) mainly localised in the endoplasmic reticulum (ER) is involved in increasing tolerance to chilling.
Results: A higher transcription level of OsSHMT was detected in Lsi1-OX rice than in the wild type. Histone H1 and nucleic acid binding protein were found to bind to the promoter region of OsSHMT and regulate its expression, and the transcription levels of these proteins were also up-regulated in the Lsi1-OX rice. Moreover, OsSHMT interacts with ATP synthase subunit α, heat shock protein Hsp70, mitochondrial substrate carrier family protein, ascorbate peroxidase 1 and ATP synthase subunit β. Lsi1-encoded protein OsNIP2;1 also interacts with ATP synthase subunit β, and the coordination of these proteins appears to function in reducing reactive oxygen species, as the H2O2 content of transgenic OsSHMT Arabidopsis thaliana was lower than that of the non-transgenic line under chilling treatment.
Conclusions: Our results indicate that ER-localised OsSHMT plays a role in scavenging H2O2 to enhance the chilling tolerance of Lsi1-OX rice and that ATP synthase subunit β is an intermediate junction between OsNIP2;1 and OsSHMT.
Figure 1
Figure 2
Figure 3
Figure 4
Figure 5
Figure 6
Figure 7
Figure 8