High CO2 Requiring Mutant of Anacystis nidulans R2
نویسندگان
چکیده
منابع مشابه
Anacystis nidulans
Three independently isolated ultraviolet light-sensitive (uvs) mutants of Anacystis nidulans were characterized. Strain uvs-1 was most sensitive to UV in the absence of photoreactivation. Pretreatment with caffeine suppressed the dark-survival curve of strain uvs-1, indicating the presence of excision enzymes involved in dark repair. Under "black" and "white" illumination, strain uvs-1 displays...
متن کاملOrganization of pigment proteins in the photosystem II complex of the cyanobacterium Anacystis nidulans R2.
Two chlorophyll-protein complexes associated with photosystem II (PSII) of the cyanobacterium Anacystis nidulans R2 have been detected. The larger of the two complexes, CPVI-1, contained a 71-kDa and a 42-kDa protein. The 71-kDa protein was determined to be the anchor protein of the phycobilisomes (the light-harvesting complex of A. nidulans PSII), since it was recognized by an antibody raised ...
متن کاملImmunological Characterization of Iron-Regulated Membrane Proteins in the Cyanobacterium Anacystis nidulans R2.
Antibodies cross-reactive with specific membrane proteins were used to investigate membrane development in Anacystis nidulans R2 during recovery from iron stress. Polyclonal antibodies prepared using the iron-regulated chlorophyll (Chl)-protein CPVI-4 (HB Pakrasi, HC Riethman, LA Sherman 1985 Proc Natl Acad Sci USA 82: 6903-6907) as antigen were characterized and used to identify three iron str...
متن کاملIdentification and Purification of a Derepressible Alkaline Phosphatase from Anacystis nidulans R2.
We have examined the increase in alkaline phosphatase activity in the cyanobacterium Anacystis nidulans R2 upon phosphate deprivation. Much of the activity is released into the medium when A. nidulans is osmotically shocked, indicating that the enzyme is located either in the periplasmic space or is loosely bound to the cell wall. The polypeptide associated with phosphatase activity has been id...
متن کاملCrystallographic characterization of flavodoxin from Anacystis nidulans.
Flavodoxin isolated from the blue-green alga, Anmyatis nidulana, crystallizes from ammonium sulfate in space group P2,2,2,, wwith a = 67.08 A, b = 69.24 A and c = 45.55 A. The diffraction patterns extend to a resolution of at least 1.8 A. Reduction of the flavin mononucleotide in the crystalline protein, to either the semi-quinone or fully reduced (hydroquinone) state, results in minimal change...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Plant Physiology
سال: 1986
ISSN: 0032-0889,1532-2548
DOI: 10.1104/pp.82.2.610