Isolation and Study of Mutants Lacking a Derepressible Phosphatase in CHLAMYDOMONAS REINHARDI
AUTOR(ES)
Matagne, R. F.
RESUMO
In the green alga Chlamydomonas reinhardi, removal of inorganic phosphate from the culture medium results in the increase of phosphatase activity (derepression) in the wild-type (WT) strain as well as in a double mutant (P2Pa) lacking the two main constitutive acid phosphatases. Following treatment of WT and P2Pa with N-methyl-N'-nitro-N-nitrosoguanidine (MNNG), mutants were recovered which display very low phosphatase activities when grown in the absence of phosphate; as shown by electrophoresis, they lack one non-migrating phosphatase (PD mutants). This enzyme is active over a wide range of pH with an optimum at pH 7.5. The comparison of electropherograms from WT and mutants grown on media with or without phosphate allowed us to provide a tentative definition of the pool of derepressible phosphatases in Chlamydomonas : in addition to the neutral phosphatase lacking in PD mutants, Chlamydomonas produces two electrophoretic forms of alkaline phosphatase showing an optimal activity at pH 9.5.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=1213324Documentos Relacionados
- Phosphatase of Chlamydomonas reinhardi: biochemical and cytochemical approach with specific mutants.
- Mutants of the Biological Clock in CHLAMYDOMONAS REINHARDI
- Diploids of Clock Mutants of CHLAMYDOMONAS REINHARDI
- A mutant strain of Chlamydomonas reinhardi lacking ribulose diphosphate carboxylase activity.
- Recombinants between Clock Mutants of CHLAMYDOMONAS REINHARDI
