TY - JOUR
T1 - Stress response of plant H+-PPase-expressing transgenic Escherichia coli and Saccharomyces cerevisiae
T2 - A potentially useful mechanism for the development of stress-tolerant organisms
AU - Yoon, Ho Sung
AU - Kim, Saeng Young
AU - Kim, Il Sup
PY - 2013/2
Y1 - 2013/2
N2 - The simple proton-translocating inorganic pyrophosphatase (H+-PPase) found in plants and protists is an evolutionally conserved, essential enzyme that catalyzes the hydrolysis of pyrophosphate (PPi). Little is known about the functional contribution of H+-PPase to the cellular response to abiotic stresses, except its high salinity and drought stress. To investigate the role of H+-PPase during response to cellular stress, we isolated the cDNA of Arabidopsis thaliana H+-PPase (AVP1) and Oryza sativa H+-PPase (OVP1) and constructed transgenic Saccharomyces cerevisiae and Escherichia coli lines that express AVP1 and OVP1. In S. cerevisiae, the expression of a chimeric derivative of the AVP1 and OVP1 alleviated the phenotype associated with ipp2-deficient cells in the presence of high salinity (NaCl) and metal stressors (Cd, Mn, and Zn). In E. coli, AVP1 and OVP1 overexpression conferred enhanced tolerance to abiotic stresses, including heat shock and H2O2, as well as NaCl, Cd, Mn, Zn, Ca, and Al. Interestingly, AVP1 and OVP1 overexpression resulted in hypersensitivity to menadione and cobalt. These results demonstrate the cellular capacity of AVP1- and OVP1-expressing transgenic yeast and E. coli in response to physiological, abiotic stresses. Moreover, our results suggest new ways of engineering stress-tolerant plants that are capable of responding to climate change. Here, we provide an outline of an experimental system to examine the alternative roles of plant H+-PPase.
AB - The simple proton-translocating inorganic pyrophosphatase (H+-PPase) found in plants and protists is an evolutionally conserved, essential enzyme that catalyzes the hydrolysis of pyrophosphate (PPi). Little is known about the functional contribution of H+-PPase to the cellular response to abiotic stresses, except its high salinity and drought stress. To investigate the role of H+-PPase during response to cellular stress, we isolated the cDNA of Arabidopsis thaliana H+-PPase (AVP1) and Oryza sativa H+-PPase (OVP1) and constructed transgenic Saccharomyces cerevisiae and Escherichia coli lines that express AVP1 and OVP1. In S. cerevisiae, the expression of a chimeric derivative of the AVP1 and OVP1 alleviated the phenotype associated with ipp2-deficient cells in the presence of high salinity (NaCl) and metal stressors (Cd, Mn, and Zn). In E. coli, AVP1 and OVP1 overexpression conferred enhanced tolerance to abiotic stresses, including heat shock and H2O2, as well as NaCl, Cd, Mn, Zn, Ca, and Al. Interestingly, AVP1 and OVP1 overexpression resulted in hypersensitivity to menadione and cobalt. These results demonstrate the cellular capacity of AVP1- and OVP1-expressing transgenic yeast and E. coli in response to physiological, abiotic stresses. Moreover, our results suggest new ways of engineering stress-tolerant plants that are capable of responding to climate change. Here, we provide an outline of an experimental system to examine the alternative roles of plant H+-PPase.
KW - Escherichia coli
KW - Heterologous expression
KW - Inorganic pyrophosphatase
KW - Saccharomyces cerevisiae
KW - Stress response
UR - http://www.scopus.com/inward/record.url?scp=84872654805&partnerID=8YFLogxK
U2 - 10.1007/s13353-012-0117-x
DO - 10.1007/s13353-012-0117-x
M3 - Article
C2 - 23055406
AN - SCOPUS:84872654805
SN - 1234-1983
VL - 54
SP - 129
EP - 133
JO - Journal of Applied Genetics
JF - Journal of Applied Genetics
IS - 1
ER -