Tobacco aquaporin NtAQP1 and human aquaporin hAQP1 contribute to single cell photosynthesis in Synechococcus.

Background Information: Aquaporins are HO-permeable membrane protein pores. However, some aquaporins are also permeable to other substances such as CO. In higher plants, overexpression of such aquaporins has already led to an enhanced photosynthetic performance due to improved CO mesophyll conductance.

Impacts of Radio-Frequency Electromagnetic Field (RF-EMF) on Lettuce ()-Evidence for RF-EMF Interference with Plant Stress Responses.

The increased use of wireless technology causes a significant exposure increase for all living organisms to radio frequency electromagnetic fields (RF-EMF). This comprises bacteria, animals, and also plants. Unfortunately, our understanding of how RF-EMF influences plants and plant physiology remains inadequate.

Metabolic engineering of ketocarotenoids biosynthetic pathway in Chlamydomonas reinhardtii strain CC-4102.

In Chlamydomonas reinhardtii, ketocarotenoid biosynthesis is limited to the diploid zygospore stage. In this study, we attempted to engineer the ketocarotenoid pathway into Chlamydomonas haploid vegetative green cells by overexpressing the key enzyme ß-carotene ketolase (CrBKT). We chose strain CC-4102 for the approach; competitive pathways, α-carotene biosynthesis and xanthophyll cycle are silenced in this strain.

Co-Translational Insertion of Aquaporins into Liposome for Functional Analysis via an Based Cell-Free Protein Synthesis System.

Aquaporins are important and well-studied water channel membrane proteins. However, being membrane proteins, sample preparation for functional analysis is tedious and time-consuming. In this paper, we report a new approach for the co-translational insertion of two aquaporins from and using the CFPS system.

Aquaporin PIP2;1 affects water transport and root growth in rice (Oryza sativa L.).

Aquaporins are key proteins in regulating water transport, plant growth and development. In this study, we investigated the function of plasma membrane intrinsic proteins (PIPs) in both yeast (Saccharomyces cerevisiae) and rice (Oryza sativa cv. Nipponbare).