Ontology type: schema:ScholarlyArticle Open Access: True
2011-04-05
AUTHORSTerry A. Krulwich, George Sachs, Etana Padan
ABSTRACTKey PointsBacteria that grow optimally in a pH range of near neutral (neutralophiles) require robust mechanisms for cytoplasmic pH homeostasis in order to survive, and in some cases grow, during exposure to acidic or alkaline conditions that are well outside the pH range tolerated for cytoplasmic pH. Extremely acidophilic bacteria maintain a cytoplasmic pH of ∼6.0 while growing at pH 1.0–3.0 in settings such as mining and geothermal areas or acidic soils, and extremely alkaliphilic bacteria maintain a cytoplasmic pH that is as much as 2.3 units below an external pH range of 9.5–11.0 in settings such as alkaline soda lakes, indigo dye plants and sewage plants.Active mechanisms of pH homeostasis under acid challenge conditions include increased expression and activity of proteins or pathways that result in outward proton pumping or the consumption of cytoplasmic protons. Under alkali challenge conditions, mechanisms of pH homeostasis include active proton accumulation or generation in the cytoplasm. Deployment of these strategies and passive adjuncts to the active strategies, such as alterations in membrane permeability to protons, require major transcriptome changes that are mediated by an intricate network of pH-sensing and signalling capabilities.The Na+/H+ antiporter of Escherichia coli, NhaA, is required for alkaline pH homeostasis in the presence of Na+; in addition to its catalytic capacity to support cytoplasmic proton accumulation at high pH, the antiporter protein possesses a pH sensor domain that results in an increase in antiport by three orders of magnitude as the pH is raised from 6.5 to 8.5. Structural studies of three-dimensional crystals of purified NhaA, combined with computational and experimental analyses, have revealed structural and mechanistic features that account for its physiological efficacy.Periplasmic pH homeostasis is a unique strategy among neutralophiles. It enables Helicobacter pylori to colonize the highly acidic surface of the stomach using urease, an acid-gated urea channel (UreI) and cytoplasmic and periplasmic carbonic anhydrases to maintain a periplasmic pH of ∼6.1. The pH gating of UreI involves hydrogen bonding of periplasmic histidines with periplasmic carboxylates. A pair of two-component pH-signalling systems play critical parts in urease trafficking to the inner membrane, where, together with UreI, the enzyme facilitates urea hydrolysis and direct export of the products (CO2, NH3 and NH4+) to the periplasm.Acidophiles and alkaliphiles that grow optimally at extreme pH values typically have adaptations to key proton-translocating complexes (for example, respiratory and ATP synthase complexes) and to their cell surface layers, as reflected by the high and low average isoelectric points, respectively, of their surface-exposed proteins relative to those of the surface-exposed proteins of neutralophiles. These constitutive adaptations promote optimal function at extreme pH, but reduce the growth capacity at near-neutral pH, as shown for the adaptations of the proton-translocating ATP synthase and highly expressed S-layer protein of alkaliphilic Bacillus pseudofirmus OF4.Much has been learned about individual strategies for bacterial pH homeostasis and the molecules involved, but bacterial pH homeostasis is a cell-wide physiological process that deploys and integrates these strategies differently depending on other environmental factors, such as oxygen availability and salinity. The development of systems-level models will depend on further efforts to gather broad-based quantitative 'omics' information as a function of pH under different conditions, and also on more detailed molecular information about the stoichiometric, kinetic and mechanistic properties of key transporters and enzymes. More... »
PAGES330-343
http://scigraph.springernature.com/pub.10.1038/nrmicro2549
DOIhttp://dx.doi.org/10.1038/nrmicro2549
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64 | ″ | ″ | bacteria |
65 | ″ | ″ | bonding |
66 | ″ | ″ | capability |
67 | ″ | ″ | capacity |
68 | ″ | ″ | carbonic |
69 | ″ | ″ | carboxylate |
70 | ″ | ″ | cases |
71 | ″ | ″ | catalytic capacity |
72 | ″ | ″ | cell surface layers |
73 | ″ | ″ | challenge conditions |
74 | ″ | ″ | changes |
75 | ″ | ″ | channels |
76 | ″ | ″ | coli |
77 | ″ | ″ | complexes |
78 | ″ | ″ | conditions |
79 | ″ | ″ | constitutive adaptation |
80 | ″ | ″ | consumption |
81 | ″ | ″ | critical part |
82 | ″ | ″ | crystals |
83 | ″ | ″ | cytoplasm |
84 | ″ | ″ | cytoplasmic |
85 | ″ | ″ | cytoplasmic pH |
86 | ″ | ″ | cytoplasmic protons |
87 | ″ | ″ | deployment |
88 | ″ | ″ | detailed molecular information |
89 | ″ | ″ | development |
90 | ″ | ″ | different conditions |
91 | ″ | ″ | direct export |
92 | ″ | ″ | domain |
93 | ″ | ″ | dye plants |
94 | ″ | ″ | efficacy |
95 | ″ | ″ | efforts |
96 | ″ | ″ | environmental factors |
97 | ″ | ″ | enzyme |
98 | ″ | ″ | experimental analysis |
99 | ″ | ″ | export |
100 | ″ | ″ | exposure |
101 | ″ | ″ | expression |
102 | ″ | ″ | external pH range |
103 | ″ | ″ | extreme pH |
104 | ″ | ″ | factors |
105 | ″ | ″ | features |
106 | ″ | ″ | function |
107 | ″ | ″ | further efforts |
108 | ″ | ″ | gating |
109 | ″ | ″ | generation |
110 | ″ | ″ | geothermal area |
111 | ″ | ″ | growth capacity |
112 | ″ | ″ | high pH |
113 | ″ | ″ | histidine |
114 | ″ | ″ | homeostasis |
115 | ″ | ″ | hydrogen bonding |
116 | ″ | ″ | hydrolysis |
117 | ″ | ″ | increase |
118 | ″ | ″ | individual strategies |
119 | ″ | ″ | information |
120 | ″ | ″ | inner membrane |
121 | ″ | ″ | intricate network |
122 | ″ | ″ | isoelectric point |
123 | ″ | ″ | key transporters |
124 | ″ | ″ | lakes |
125 | ″ | ″ | layer |
126 | ″ | ″ | magnitude |
127 | ″ | ″ | major transcriptome changes |
128 | ″ | ″ | mechanism |
129 | ″ | ″ | mechanistic features |
130 | ″ | ″ | mechanistic properties |
131 | ″ | ″ | membrane |
132 | ″ | ″ | membrane permeability |
133 | ″ | ″ | mining |
134 | ″ | ″ | model |
135 | ″ | ″ | molecular aspects |
136 | ″ | ″ | molecular information |
137 | ″ | ″ | molecules |
138 | ″ | ″ | network |
139 | ″ | ″ | neutral pH |
140 | ″ | ″ | neutralophile |
141 | ″ | ″ | omics information |
142 | ″ | ″ | optimal function |
143 | ″ | ″ | order |
144 | ″ | ″ | orders of magnitude |
145 | ″ | ″ | oxygen availability |
146 | ″ | ″ | pH |
147 | ″ | ″ | pH gating |
148 | ″ | ″ | pH homeostasis |
149 | ″ | ″ | pH range |
150 | ″ | ″ | pH sensing |
151 | ″ | ″ | pairs |
152 | ″ | ″ | part |
153 | ″ | ″ | pathway |
154 | ″ | ″ | periplasm |
155 | ″ | ″ | periplasmic |
156 | ″ | ″ | periplasmic pH |
157 | ″ | ″ | permeability |
158 | ″ | ″ | physiological efficacy |
159 | ″ | ″ | physiological processes |
160 | ″ | ″ | plants |
161 | ″ | ″ | point |
162 | ″ | ″ | presence |
163 | ″ | ″ | process |
164 | ″ | ″ | products |
165 | ″ | ″ | properties |
166 | ″ | ″ | protein |
167 | ″ | ″ | proton accumulation |
168 | ″ | ″ | proton pumping |
169 | ″ | ″ | proton-translocating ATP synthase |
170 | ″ | ″ | proton-translocating complex |
171 | ″ | ″ | protons |
172 | ″ | ″ | pumping |
173 | ″ | ″ | pylori |
174 | ″ | ″ | quantitative |
175 | ″ | ″ | range |
176 | ″ | ″ | robust mechanism |
177 | ″ | ″ | salinity |
178 | ″ | ″ | sensing |
179 | ″ | ″ | sensor domain |
180 | ″ | ″ | setting |
181 | ″ | ″ | sewage plant |
182 | ″ | ″ | soda lakes |
183 | ″ | ″ | soil |
184 | ″ | ″ | stomach |
185 | ″ | ″ | strategies |
186 | ″ | ″ | structural studies |
187 | ″ | ″ | study |
188 | ″ | ″ | surface |
189 | ″ | ″ | surface layer |
190 | ″ | ″ | surface-exposed proteins |
191 | ″ | ″ | synthase |
192 | ″ | ″ | system |
193 | ″ | ″ | system-level model |
194 | ″ | ″ | three-dimensional crystals |
195 | ″ | ″ | transcriptome changes |
196 | ″ | ″ | transporters |
197 | ″ | ″ | unique strategy |
198 | ″ | ″ | units |
199 | ″ | ″ | urea channel |
200 | ″ | ″ | urea hydrolysis |
201 | ″ | ″ | urease |
202 | ″ | ″ | values |
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