Abstract

Increased expression of the aquaporin NtAQP1, which is known to function as a plasmalemma channel for CO2 and water, increases the rate of both photosynthesis and transpiration. In contrast, increased expression of Arabidopsis hexokinase1 (AtHXK1), a dual-function enzyme that mediates sugar sensing, decreases the expression of photosynthetic genes and the rate of transpiration and inhibits growth. Here, we show that AtHXK1 also decreases root and stem hydraulic conductivity and leaf mesophyll CO2 conductance (g m). Due to their opposite effects on plant development and physiology, we examined the relationship between NtAQP1 and AtHXK1 at the whole-plant level using transgenic tomato plants expressing both genes simultaneously. NtAQP1 significantly improved growth and increased the transpiration rates of AtHXK1-expressing plants. Reciprocal grafting experiments indicated that this complementation occurs when both genes are expressed simultaneously in the shoot. Yet, NtAQP1 had only a marginal effect on the hydraulic conductivity of the double-transgenic plants, suggesting that the complementary effect of NtAQP1 is unrelated to shoot water transport. Rather, NtAQP1 significantly increased leaf mesophyll CO2 conductance and enhanced the rate of photosynthesis, suggesting that NtAQP1 facilitated the growth of the double-transgenic plants by enhancing mesophyll conductance of CO2.

Highlights

  • Aquaporins (AQPs), known as MIPs, are integral membrane proteins that increase the permeability of membranes to water, as well as small uncharged molecules [1]

  • In light of the opposite effects of AtHXK1 and NtAQP1 on photosynthesis and growth, we examined the relationship between AtHXK1 and NtAQP1 using doubletransgenic plants that express AtHXK1 and NtAQP1 simultaneously

  • We found that NtAQP1 significantly compensated for the growth inhibition imposed by AtHXK1, primarily by enhancing mesophyll CO2 conductance and the rate of photosynthesis, while the hydraulic conductivity in those plants remained unchanged

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Summary

Introduction

Aquaporins (AQPs), known as MIPs (major intrinsic proteins), are integral membrane proteins that increase the permeability of membranes to water, as well as small uncharged molecules [1]. AQPs have been divided into five subgroups: plasma membrane intrinsic proteins (PIPs), tonoplast intrinsic proteins (TIPs), NOD26-like intrinsic proteins (NIPs), small basic intrinsic proteins (SIPs) and X intrinsic proteins (XIP) [4,6]. Plant PIPs can be divided into two major groups, PIP1 and PIP2, on the basis of their sequences and water-channel activity. PIP2 proteins exhibit high levels of water-channel activity in Xenopus oocytes and yeast vesicles; whereas PIP1 proteins often have relatively low permeability to water [7,8,9,10,11,12]

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