For Publishers
DiscoveryMetadataPeer reviewHostingPublishing
For Researchers
JoinPublishReviewCollect
Register
Blog
About
Search
Advanced search
My ScienceOpen
Search
For Publishers
For Researchers
Blog
About
7
views
80
references
 Top references
cited by
36
    
0 reviews
 Review
0
comments
 Comment
0
recommends
+1 Recommend
0 collections
    0
    shares
      377
      similar
       All similar
      • Record: found
      • Abstract: found
      • Article: found
      Is Open Access

      Salinity Stress Responses and Adaptation Mechanisms in Eukaryotic Green Microalgae

      review-article

      Read this article at

      ScienceOpenPublisherPMC
      Bookmark
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          Abstract

          High salinity is a challenging environmental stress for organisms to overcome. Unicellular photosynthetic microalgae are especially vulnerable as they have to grapple not only with ionic imbalance and osmotic stress but also with the generated reactive oxygen species (ROS) interfering with photosynthesis. This review attempts to compare and contrast mechanisms that algae, particularly the eukaryotic Chlamydomonas microalgae, exhibit in order to immediately respond to harsh conditions caused by high salinity. The review also collates adaptation mechanisms of freshwater algae strains under persistent high salt conditions. Understanding both short-term and long-term algal responses to high salinity is integral to further fundamental research in algal biology and biotechnology.

          Related collections

          Most cited references80

          • Record: found
          • Abstract: not found
          • Article: not found

          Effects of salt stress on basic processes of photosynthesis

          S.D.S. Murthy, P. Sudhir (2004)
          Article 0 comments Cited 119 times – based on 0 reviews     Review now
            Bookmark
            • Record: found
            • Abstract: found
            • Article: not found

            Why is trehalose an exceptional protein stabilizer? An analysis of the thermal stability of proteins in the presence of the compatible osmolyte trehalose.

            Jai K. Kaushik, Rajiv Bhat (2003)
            Trehalose, a naturally occurring osmolyte, is known to be an exceptional stabilizer of proteins and helps retain the activity of enzymes in solution as well as in the freeze-dried state. To understand the mechanism of action of trehalose in detail, we have conducted a thorough investigation of its effect on the thermal stability in aqueous solutions of five well characterized proteins differing in their various physico-chemical properties. Among them, RNase A has been used as a model enzyme to investigate the effect of trehalose on the retention of enzymatic activity upon incubation at high temperatures. 2 m trehalose was observed to raise the transition temperature, Tm of RNase A by as much as 18 degrees C and Gibbs free energy by 4.8 kcal mol-1 at pH 2.5. There is a decrease in the heat capacity of protein denaturation (DeltaCp) in trehalose solutions for all the studied proteins. An increase in the DeltaG and a decrease in the DeltaCp values for all the proteins points toward a general mechanism of stabilization due to the elevation and broadening of the stability curve (DeltaG versus T). A direct correlation of the surface tension of trehalose solutions and the thermal stability of various proteins has been observed. Wyman linkage analysis indicates that at 1.5 m concentration 4-7 molecules of trehalose are excluded from the vicinity of protein molecules upon denaturation. We further show that an increase in the stability of proteins in the presence of trehalose depends upon the length of the polypeptide chain. The pH dependence data suggest that even though the charge status of a protein contributes significantly, trehalose can be expected to work as a universal stabilizer of protein conformation due to its exceptional effect on the structure and properties of solvent water compared with other sugars and polyols.
            Article 0 comments Cited 81 times – based on 0 reviews     Review now
              Bookmark
              • Record: found
              • Abstract: found
              • Article: not found

              Proline accumulation and salt-stress-induced gene expression in a salt-hypersensitive mutant of Arabidopsis.

              Jie Zhu, L. Liu (1997)
              The sos1 mutant of Arabidopsis thaliana is more than 20 times more sensitive to NaCl stress than wild type Arabidopsis. Because proline (Pro) is generally thought to have an important role in plant salt tolerance, the sos1 mutant and the wild type were compared with respect to their capacity to accumulate Pro under NaCl stress, and sos1 mutant plants accumulated more Pro than wild-type. The P5CS gene, which catalyzes the rate-limiting step in Pro biosynthesis, is induced by salt stress to a higher level in sos1 than in the wild type. Although a defective high-affinity K uptake system in sos1 causes K deficiency and inhibits growth in NaCl-treated plants, this decrease is not a sufficient signal for Pro accumulation and P5CS gene expression. Not all salt-stress-induced genes have a higher level of expression in sos1. The expression levels of AtPLC and RD29A, which encode a phospholipase C homolog and a putative protective protein, respectively, are the same in sos1 as in the wild type. However, the expression of AtMYB, which encodes a putative transcriptional factor, is induced to a much higher level by salt stress in sos1. Thus, the SOS1 gene product serves as a negative regulator for the expression of P5CS and AtMYB, but has no effect on AtPLC and RD29A expression.
              Article 0 comments Cited 74 times – based on 0 reviews     Review now
                Bookmark
                All references

                Author and article information

                Journal
                Journal ID (nlm-ta): Cells
                Journal ID (iso-abbrev): Cells
                Journal ID (publisher-id): cells
                Title: Cells
                Publisher: MDPI
                ISSN (Electronic): 2073-4409
                Publication date (Electronic): 17 December 2019
                Publication date Collection: December 2019
                Volume: 8
                Issue: 12
                Electronic Location Identifier: 1657
                Affiliations
                [1 ]Institute of Plant Biology, Hungarian Academy of Sciences, Biological Research Centre, 6726 Szeged, Hungary; shettypr@ 123456brc.hu (P.S.); gitau.margaret@ 123456brc.hu (M.M.G.)
                [2 ]Faculty of Water Sciences, National University of Public Service, 6500 Baja, Hungary
                Author notes
                [* ]Correspondence: maroti.gergely@ 123456brc.hu ; Tel.: +36-308-270455
                Author information
                https://orcid.org/0000-0002-3705-0461
                Article
                Publisher ID: cells-08-01657
                DOI: 10.3390/cells8121657
                PMC ID: 6952985
                PubMed ID: 31861232
                SO-VID: efdfdb95-47a2-4c07-9787-a0fd0f506ddf
                Copyright © © 2019 by the authors.
                License:

                Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license ( http://creativecommons.org/licenses/by/4.0/).

                History
                Date received : 01 October 2019
                Date accepted : 12 December 2019
                Categories
                Subject: Review

                Keywords: high salt stress,green algae,adaptation,transcriptome,salinity,chlamydomonas
                Data availability:
                Keywords: high salt stress, green algae, adaptation, transcriptome, salinity, chlamydomonas

                Comments

                Comment on this article

                scite_

                Similar content377

                See all similar

                Cited by36

                See all cited by

                Most referenced authors664

                See all reference authors