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1.
Ying Yong Sheng Tai Xue Bao ; 22(2): 331-6, 2011 Feb.
Article in Chinese | MEDLINE | ID: mdl-21608243

ABSTRACT

By using soil core sampling method, this paper studied the soil moisture regime of rubber plantations and the fine root biomass of Hevea brasiliensis in immature period (5 a), early yielding period (9 a), and peak yielding period (16 a). With the increasing age of rubber trees, the soil moisture content of rubber plantations increased but the fine root biomass decreased. The soil moisture content at the depth of 0-60 cm in test rubber plantations increased with soil depth, and presented a double-peak pattern over the period of one year. The fine root biomass of rubber trees at different ages had the maximum value in the top 10 cm soil layers and decreased with soil depth, its seasonal variation also showed a double-peak pattern, but the peak values appeared at different time. Soil moisture content and soil depth were the main factors affecting the fine root biomass of H. brasiliensis.


Subject(s)
Biomass , Hevea/growth & development , Plant Roots/growth & development , Soil/analysis , Water/analysis , China , Ecosystem , Hevea/anatomy & histology , Plant Roots/anatomy & histology , Time Factors
2.
J Microbiol ; 46(4): 415-21, 2008 Aug.
Article in English | MEDLINE | ID: mdl-18758732

ABSTRACT

A gene encoding a Na(+)/H(+) antiporter was obtained from the genome of Halobacillus aidingensis AD-6(T), which was sequenced and designated as nhaH. The deduced amino acid sequence of the gene was 91% identical to the NhaH of H. dabanensis, and shared 54% identity with the NhaG of Bacillus subtilis. The cloned gene enable the Escherichia coli KNabc cell, which lack all of the major Na(+)/H(+) antiporters, to grow in medium containing 0.2 M NaCl or 10 mM LiCl. The nhaH gene was predicted to encode a 43.5 kDa protein (403 amino acid residues) with 11 putative transmembrane regions. Everted membrane vesicles prepared from E. coli KNabc cells carrying NhaH exhibited Na(+)/H(+) as well as Li(+)/H(+) antiporter activity, which was pH-dependent with the highest activity at pH 8.0, and no K(+)/H(+) antiporter activity was detected. The deletion of hydrophilic C-terminal amino acid residues showed that the short C-terminal tail was vital for Na(+)/H(+) antiporter activity.


Subject(s)
Bacillaceae/genetics , Bacillaceae/metabolism , Bacterial Proteins/metabolism , Cloning, Molecular , Sodium Chloride/metabolism , Sodium-Hydrogen Exchangers/metabolism , Amino Acid Sequence , Bacillaceae/chemistry , Bacterial Proteins/chemistry , Bacterial Proteins/genetics , Base Sequence , Cell Membrane/chemistry , Cell Membrane/genetics , Cell Membrane/metabolism , Escherichia coli/genetics , Escherichia coli/metabolism , Molecular Sequence Data , Sequence Alignment , Sequence Deletion , Sodium-Hydrogen Exchangers/chemistry , Sodium-Hydrogen Exchangers/genetics
3.
Wei Sheng Wu Xue Bao ; 47(5): 937-41, 2007 Oct.
Article in Chinese | MEDLINE | ID: mdl-18062278

ABSTRACT

Moderately halophilic bacteria which grow best in media with 3% to 15% salt constitute a heterogenous group of microorganisms which belong to different genera. These bacteria can inhabit the salt or soda lakes, coastal lagoons or man-made salterns. Moderately halophilc bacteria living in higher saline environments can not only cope with high osmotic stress but also adapt osmotic shock in short time. To adapt to these environments, all the species make a osmoprotection by the accumulation a restricted range of low molecular mass molecules, small, organic compatible solutes, such as sugars, amino acids, betaines and ectoines. Therefore, the osmoadaptation of moderately halophilc bacteria is regulated by the so-called "compatible solute" strategy. Compatible solutes are operationally defined as organic osmolytes that can be amassed by the cell in exceedingly high concentrations without disturbing vital cellular functions and the correct folding of proteins. As a result, compatible solutes can make important contributions to the restoration of the turgor under conditions of low water activity by counteracting the efflux of water from the cell. In addition, they have a stabilizing, both in vivo and vitro, on the native structure of proteins and cell components. This mechanism has a minimal requirement for genetic change and a high degree of flexibility in allowing moderate halophiles to adapt to saline environment. In this review, the adaptation to saline environments, the variety and characteristic of compatible solutes, and the functional mechanism of moderately halophilic bacteria are reviewed and discussed.


Subject(s)
Bacteria/growth & development , Adaptation, Physiological , Amino Acids/metabolism , Amino Acids, Diamino/metabolism , Bacteria/metabolism , Betaine/metabolism , Carbohydrate Metabolism , Sodium Chloride/pharmacology
4.
Curr Microbiol ; 54(1): 20-6, 2007 Jan.
Article in English | MEDLINE | ID: mdl-17171470

ABSTRACT

Two-dimensional (2-D) gel electrophoresis was employed to display the expression profiles of proteins of Halobacillus dabanensis D-8(T) under 1%, 10%, and 20% salinities. Approximately 700 protein spots could be detected in the 2-D gels by Imagemastertrade mark 2D Platinum software. The molecular masses of the majority of intracellular proteins were distributed in the range of 17.5 kDa-66 kDa and isoelectric points of 4.0-5.9. In total 133 protein spots were observed with a changed expression level under different salinity conditions. Sixty-two protein spots showed upregulation and 26 new protein spots were found under high salinity conditions, while 25 protein spots were downregulated and 20 spots disappeared. Twenty-seven proteins with a markedly changed expression in hypersaline environments were identified by matrix-assisted laser desorption/ionization time-of-flight mass spectroscopy (MALDI-TOF/MS) and MASCOT. A changed expression pattern was observed for proteins related to energy-producing pathways, stress regulators, and proteins involved in the survival of strain D-8(T) under high salt challenges. Many proteins play necessary roles in the adaptation to high salt or as a general stress protein, and some proteins are salt-stressed specific proteins that improve the capability of salt-tolerance of strain D-8(T) growth under extremely hypersaline condition.


Subject(s)
Bacillaceae/metabolism , Bacterial Proteins/genetics , Gene Expression Regulation, Bacterial , Proteomics/methods , Sodium Chloride/analysis , Bacillaceae/genetics , Bacterial Proteins/chemistry , Down-Regulation , Electrophoresis, Gel, Two-Dimensional , Isoelectric Point , Molecular Weight , Software , Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization , Up-Regulation
5.
Wei Sheng Wu Xue Bao ; 47(6): 1110-4, 2007 Dec.
Article in Chinese | MEDLINE | ID: mdl-18271276

ABSTRACT

Sodium ion with high concentration is toxic to living cells, and microorganisms adapt to the environment containing high concentration of salt by the strategies of salt-in-cytoplasm and compatible solutes. The Na+ extrusion system plays important roles in maintaining cytoplasmic Na+ homeostasis and pH level in microbial cells. Two possible mechanisms of Na+ circulation across the cytoplasmic membrane have been proposed, namely primary Na+ pump and secondary Na+/H+ antiporter. Primary sodium pumps coupled the extrusion of Na+ to respiration, and the activity of which was insensitive to uncoupler CCCP ( carbonyl-cyanide m-chlorophenylhydrazone). There were two types of secondary Na+/H+ antiporters-encoding genes designated single gene and multiple subunits, respectively. The types of transportation systems for Na+, possible mechanisms of Na+ extrusion, and projects for further study in bacteria are reviewed.


Subject(s)
Bacteria/metabolism , Sodium/immunology , Ion Transport , Sodium-Hydrogen Exchangers/physiology , Sodium-Potassium-Exchanging ATPase/physiology
6.
FEMS Microbiol Lett ; 255(1): 89-95, 2006 Feb.
Article in English | MEDLINE | ID: mdl-16436066

ABSTRACT

A gene encoding a Na(+)/H(+) antiporter was cloned from a chromosomal DNA of Halobacillus dabanensis strain D-8(T) by functional complementation. Its presence enabled the antiporter-deficient Escherichia coli strain KNabc to survive in the presence of 0.2 M NaCl or 5 mM LiCl. The gene was sequenced and designated as nhaH. The deduced amino-acid sequence of NhaH consists of 403 residues with a calculated molecular mass of 43,481 Da, which was 54% identical and 76% similar to the NhaG Na(+)/H(+) antiporter of Bacillus subtilis. The hydropathy profile was characteristic of a membrane protein with 12 putative transmembrane domains. Everted membrane vesicles prepared from E. coli cells carrying nhaH exhibited Na(+)/H(+) as well as Li(+)/H(+) antiporter activity, which was pH-dependent with highest activities at pH 8.5-9.0 and at pH 8.5, respectively. Moreover, nhaH confers upon E. coli KNabc cells the ability to grow under alkaline conditions.


Subject(s)
Bacillaceae/genetics , Sodium Chloride/metabolism , Sodium-Hydrogen Exchangers/genetics , Amino Acid Sequence , Bacillaceae/classification , Cloning, Molecular , DNA, Bacterial/analysis , Hydrogen-Ion Concentration , Molecular Sequence Data , Sequence Analysis, DNA , Sodium-Hydrogen Exchangers/metabolism
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