Crop productivity strongly depends on several biotic and abiotic factors. Salinity is one of the most important abiotic factors, besides drought, extreme temperatures, light and metal stress. The enhanced burden of secondary salinization induced through anthropogenic activities increases pressure on glycophytic crop plants. The recent isolation and characterization of salt tolerance genes encoding signaling components from halophytes, which naturally grow in high salinity, has provided tools for the development of transgenic crop plants with improved salt tolerance and economically beneficial traits. In addition understanding of the differences between glycophytes and halophytes with respect to levels of salinity tolerance is also one of the prerequisite to achieve this goal. Based on the recent developments in mechanisms of salt tolerance in halophytes, we will explore the potential of introducing salt tolerance by choosing the available genes from both dicotyledonous and monocotyledonous halophytes, including the salt overly sensitive system (SOS)-related cation/proton antiporters of plasma (NHX/SOS1) and vacuolar membranes (NHX), energy-related pumps, such as plasma membrane and vacuolar H + adenosine triphosphatase (PM & V-H + ATPase), vacuolar H + pyrophosphatases (V-H + PPase) and potassium transporter genes. Various halophyte genes responsible for other processes, such as crosstalk signaling, osmotic solutes production and reactive oxygen species (ROS) suppression, which also enhance salt tolerance will be described. In addition, the transgenic overexpression of halophytic genes in crops (rice, peanut, finger millet, soybean, tomato, alfalfa, jatropha, etc.) will be discussed as a successful mechanism for the induction of salt tolerance. Moreover, the advances in genetic engineering technology for the production of genetically modified crops to achieve the improved salinity tolerance under field conditions will also be discussed. 2015 Elsevier B.V. All rights reserved.

Photosystem I-hydrogenase chimera intercepts electron flow directly from the photosynthetic electron transport chain and directs it to hydrogen production.

Despite the impressive progress made in recent years in understanding the early steps in charge separation within the photosynthetic reaction centers, our knowledge of how ferredoxin (Fd) interacts with the acceptor side of photosystem I (PSI) is not as well developed. Fd accepts electrons after transiently docking to a binding site on the acceptor side of PSI. However, the exact location, as well as the stoichiometry, of this binding have been a matter of debate for more than two decades. Here, using Isothermal Titration Calorimetry (ITC) and purified components from wild type and mutant strains of the green algae Chlamydomonas reinhardtii we show that PSI has a single binding site for Fd, and that the association consists of two distinct binding events, each with a specific association constant.