The C‐terminus of yeast plasma membrane H<sup>+</sup>‐ATPase is essential for the regulation of this enzyme by heat shock protein Hsp30, but not for stress activation

Braley, R; Piper, Peter W.

doi:10.1016/s0014-5793(97)01359-8

Cited by 34 publications

(15 citation statements)

References 29 publications

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“…33); a hypothetical protein identified by genomic sequencing in the fission yeast Schizosaccharomyces pombe; an Hsp30 homologue from the basidiomycete Coriolus versicolor, and an incomplete sequence derived from a set of overlapping ESTs from the filamentous ascomycete Emericella nidulans. S. cerevisiae Hsp30p is an integral plasma membrane protein that down-regulates the plasma membrane H ϩ -ATPase in response to heat shock and exposure to weak acids (34). Functions for the remaining fungal proteins are unknown.…”

Section: Resultsmentioning

confidence: 99%

The nop-1 gene of Neurospora crassa encodes a seven transmembrane helix retinal-binding protein homologous to archaeal rhodopsins

Bieszke

Braun

Bean

et al. 1999

Proc. Natl. Acad. Sci. U.S.A.

208

161

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Opsins are a class of retinal-binding, seven transmembrane helix proteins that function as lightresponsive ion pumps or sensory receptors. Previously, genes encoding opsins had been identified in animals and the Archaea but not in fungi or other eukaryotic microorganisms. Here, we report the identification and mutational analysis of an opsin gene, nop-1, from the eukaryotic filamentous fungus Neurospora crassa. The nop-1 amino acid sequence predicts a protein that shares up to 81.8% amino acid identity with archaeal opsins in the 22 retinal binding pocket residues, including the conserved lysine residue that forms a Schiff base linkage with retinal. Evolutionary analysis revealed relatedness not only between NOP-1 and archaeal opsins but also between NOP-1 and several fungal opsin-related proteins that lack the Schiff base lysine residue. The results provide evidence for a eukaryotic opsin family homologous to the archaeal opsins, providing a plausible link between archaeal and visual opsins. Extensive analysis of ⌬nop-1 strains did not reveal obvious defects in light-regulated processes under normal laboratory conditions. However, results from Northern analysis support light and conidiation-based regulation of nop-1 gene expression, and NOP-1 protein heterologously expressed in Pichia pastoris is labeled by using all-trans [ 3 H]retinal, suggesting that NOP-1 functions as a rhodopsin in N. crassa photobiology.Retinal is a chromophore that binds to integral membrane proteins (opsins) to form light-absorbing pigments known as rhodopsins. Visual rhodopsins contain the chromophore 11-cis retinal, which has intrinsic qualities optimal for vision (1). In contrast, archaeal rhodopsins contain all-trans retinal and function in light-activated ion pumping and phototaxis (reviewed in ref. 2). Archaeal and visual rhodopsins show little sequence identity but possess a similar secondary structure (3). This structure includes seven transmembrane ␣-helical domains and a conserved lysine residue in the seventh helix (helix G) that forms a Schiff base linkage with retinal (4). On light absorption, the retinal isomerizes and the Schiff base is deprotonated. These events are followed by conformational changes in the opsin protein and subsequent transduction of the light signal.Four different archaeal rhodopsins have been identified in Halobacterium salinarum (reviewed in refs. 2 and 5). These are bacteriorhodopsin, (BR), halorhodopsin (HR), Sensory rhodopsin I (SRI), and sensory rhodopsin II (SRII). BR and HR are ion pumps that are activated by orange light under semianaerobic conditions; they function by expelling hydrogen ions from the cell or taking in extracellular chloride ions, respectively. The pumping action of BR and HR hyperpolarizes the membrane, driving ATP synthesis during anaerobic growth. SRI controls phototaxis of the cell to orange light during anaerobic conditions to energize pumping of BR and HR. SRII also controls cell motility but is produced only in oxygen, where it induces an avoidance response to b...

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Section: Resultsmentioning

confidence: 99%

The nop-1 gene of Neurospora crassa encodes a seven transmembrane helix retinal-binding protein homologous to archaeal rhodopsins

Bieszke

Braun

Bean

et al. 1999

Proc. Natl. Acad. Sci. U.S.A.

208

161

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“…The glucose-induced increase in the V max of the ATPase depends on Arg-909 and Thr-912, which define a potential phosphorylation site for calmodulin-dependent protein kinase II. However, mutational analysis has indicated that the mechanism of V max regulation is more complex than simple phosphorylation (12) and involves the membrane protein YOR137c (9) and the small heat shock protein Hsp30 (4). Other pieces of the puzzle of ion homeostasis in yeast include the calcium-regulated protein phosphatase calcineurin, which regulates both Trk1,2 and the ATPase (62), and, as demonstrated in fission yeast, some type I protein phosphatases and mitogen-activated protein kinases (2).…”

Section: Discussionmentioning

confidence: 99%

“…Accordingly, H ϩ -ATPase activities correlate with growth rates (42) and stress responses (4,32,39). One mechanism of plasma membrane H ϩ -ATPase regulation occurs at the transcriptional level.…”

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confidence: 99%

Regulation of Yeast H⁺-ATPase by Protein Kinases Belonging to a Family Dedicated to Activation of Plasma Membrane Transporters

Goossens

Fuente

Forment

et al. 2000

Molecular and Cellular Biology

182

193

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The regulation of electrical membrane potential is a fundamental property of living cells. This biophysical parameter determines nutrient uptake, intracellular potassium and turgor, uptake of toxic cations, and stress responses. In fungi and plants, an important determinant of membrane potential is the electrogenic protonpumping ATPase, but the systems that modulate its activity remain largely unknown. We have characterized two genes from Saccharomyces cerevisiae, PTK2 and HRK1 (YOR267c), that encode protein kinases implicated in activation of the yeast plasma membrane H ؉ -ATPase (Pma1) in response to glucose metabolism. These kinases mediate, directly or indirectly, an increase in affinity of Pma1 for ATP, which probably involves Ser-899 phosphorylation. Ptk2 has the strongest effect on Pma1, and ptk2 mutants exhibit a pleiotropic phenotype of tolerance to toxic cations, including sodium, lithium, manganese, tetramethylammonium, hygromycin B, and norspermidine. A plausible interpretation is that ptk2 mutants have a decreased membrane potential and that diverse cation transporters are voltage dependent. Accordingly, ptk2 mutants exhibited reduced uptake of lithium and methylammonium. Ptk2 and Hrk1 belong to a subgroup of yeast protein kinases dedicated to the regulation of plasma membrane transporters, which include Npr1 (regulator of Gap1 and Tat2 amino acid transporters) and Hal4 and Hal5 (regulators of Trk1 and Trk2 potassium transporters).

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“…This led to down-regulation of the stress stimulation of the H + -ATPase and suggested that the role of Hsp30 may be to conserve the cellular ATP levels under long-term stress, which would have been consumed by the enzyme while attempting to restore homeostasis. Thus, the cell must be able to balance the need for H + -ATPase activity for maintaining homeostasis and the need for appropriate ATP levels for growth in order to adapt to growth under weak acid stress (Braley and Piper 1997). Henriques and others (1997) showed evidence of an efflux system that removes accumulated anions from inside the cell.…”

Section: Effects Of Weak Acid Stress On Gene Expressionmentioning

confidence: 99%

Adaptation of Microorganisms to Cold Temperatures, Weak Acid Preservatives, Low pH, and Osmotic Stress: A Review

Beales

2004

Comp Rev Food Sci Food Safe

611

361

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The application of physical stress to microorganisms is the most widely used method to induce cell inactivation and promote food stability. To survive, microorganisms have evolved both physiological and genetic mechanisms to tolerate some extreme physical conditions. This is clearly of significance to the food industry in relation to survival of pathogens or spoilage organisms in food. In some microorganisms, the "cold shock response" has been observed in response to abrupt changes to lower temperatures. This results in the production of specific sets of proteins (cold shock proteins), the continued synthesis of proteins involved in transcription and translation, and the repression of heat shock proteins. The addition of weak acid preservatives (for example, sorbates, benzoates) also induces a specific pattern of gene expression (for example, 'Acid Tolerance Response'), which is likely to be required for optimal adaptation of bacteria to weak acid preservatives and low pH. The primary mode of the antimicrobial action of low pH is to reduce the internal cell pH (pHi) below the normal physiological range tolerated by the cell, leading to growth inhibition. Survival mechanisms involve maintaining pH homeostasis, and this is achieved by a combination of passive and active mechanisms. Microorganisms adapt to osmotic stress by accumulating non-ionic or compatible solutes such as trehalose, glycerol, sucrose, and mannitol. These compatible solutes help balance the osmotic pressure and help preserve protein function inside the cells. By understanding and controlling such mechanisms of adaptation, it may be possible to prevent growth of key microorganisms in food products.2 COMPREHENSIVE REVIEWS IN FOOD SCIENCE AND FOOD SAFETY-Vol. 3, 2004 CRFSFS: Comprehensive Reviews in Food Science and Food Safety organisms will still be metabolically active and viable if transferred to favorable conditions (Busta 1978;Abbiss 1983;Ray 1986). Preservation techniques are designed to prevent microbial growth in processed foods, by disrupting the internal environment of the cell such that growth is no longer possible.Temperature, water activity, addition of preservatives, and pH are all parameters used to inhibit or destroy microorganisms and their spores and are also used as an aid for food preservation (Marechal and others 1999). Other parameters such as heat and bacteriostatic and bactericidal agents are also used in food preservation; they are not included in this review, but have been reviewed extensively (Lindquist 1986;Hendrick and Hartl 1993;Abee and Wouters 1999;Brul and Coote 1999). Some microorganisms have evolved and are capable of rapidly adapting to a continuously changing environment, thus developing tolerance or resistance to increased "doses" of particular stresses. Different types of organism possess different inherent resistances and susceptibilities to stress. For instance, Gram-negative bacteria are regarded as being more sensitive to cold shock, chilling, and freezing than Gram-positive bacteria (Straka ...

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The C‐terminus of yeast plasma membrane H⁺‐ATPase is essential for the regulation of this enzyme by heat shock protein Hsp30, but not for stress activation

Cited by 34 publications

References 29 publications

The nop-1 gene of Neurospora crassa encodes a seven transmembrane helix retinal-binding protein homologous to archaeal rhodopsins

The nop-1 gene of Neurospora crassa encodes a seven transmembrane helix retinal-binding protein homologous to archaeal rhodopsins

Regulation of Yeast H⁺-ATPase by Protein Kinases Belonging to a Family Dedicated to Activation of Plasma Membrane Transporters

Adaptation of Microorganisms to Cold Temperatures, Weak Acid Preservatives, Low pH, and Osmotic Stress: A Review

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The C‐terminus of yeast plasma membrane H+‐ATPase is essential for the regulation of this enzyme by heat shock protein Hsp30, but not for stress activation

Cited by 34 publications

References 29 publications

The nop-1 gene of Neurospora crassa encodes a seven transmembrane helix retinal-binding protein homologous to archaeal rhodopsins

The nop-1 gene of Neurospora crassa encodes a seven transmembrane helix retinal-binding protein homologous to archaeal rhodopsins

Regulation of Yeast H+-ATPase by Protein Kinases Belonging to a Family Dedicated to Activation of Plasma Membrane Transporters

Adaptation of Microorganisms to Cold Temperatures, Weak Acid Preservatives, Low pH, and Osmotic Stress: A Review

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The C‐terminus of yeast plasma membrane H⁺‐ATPase is essential for the regulation of this enzyme by heat shock protein Hsp30, but not for stress activation

Regulation of Yeast H⁺-ATPase by Protein Kinases Belonging to a Family Dedicated to Activation of Plasma Membrane Transporters