Deoxyribonucleic acid-dependent ribonucleic acid polymerases in the dimorphic fungus Mucor rouxii.
نویسندگان
چکیده
Three forms of DNA-dependent RNA polymerase have been separated by chromatography of extracts of yeast-like cells and mycelium of the dimorphic fungus Mucor rouxii. Each of the three eznymes has been purified by means of protamine sulfate precipitation, ion exchange chromatography, affinity chromatography, and velocity sedimentation. Electrophoresis under denaturing conditions showed differences in the subunit compositions of all three purified enzymes. The properties of the enzymes from M. rouxii were similar to those of polymerases from other eukaryotic organisms. Denatured DNA was a better template than native DNA for all three enzymes but each enzyme had a distinct pattern of activities with different templates. Enzymes I and III displayed optimal activity with Mn-2gs the divalent cation and were stimulated significantly by Kcl and (NH4)2S04. Enzyme II had a greater activity with Mg-2gnd was only slightly stimulated by KCl and (NH4)2SO4. None of the enzymes were inhibited by cycloheximide or by rifampicin: all were inhibited by actinomycin C and rifampin AF/018: only enzyme II was inhibited by alpha-amanitin. No differences could be found in the properties of the same enzymes isolated from yeast-like cells or mycelium.
منابع مشابه
Thiamine and Nicotinic Acid: Anaerobic Growth Factors for Mucor Rouxii.
Bartnicki-Garcia, S. (Rutgers, the State University, New Brunswick, N. J.), and Walter J. Nickerson. Thiamine and nicotinic acid: Anaerobic growth factors for Mucor rouxii. J. Bacteriol. 82:142-148. 1961.-Mucor rouxii requires preformed thiamine and nicotinic acid for anaerobic growth. Such requirements are not manifested during aerobic incubation. Aerobically, the fungus was shown to be able t...
متن کاملCyanobacterial ribonucleic acid polymerases recognize lambda promoters.
We compared the initiation specificities in vitro of deoxyribonucleic acid-dependent ribonucleic acid polymerases purified from two cyanobacteria, Fremyella diplosiphon and Anacystis nidulans, and from Escherichia coli. A restriction fragment made from lambda deoxyribonucleic acid was used as a template. The cyanobacterial and E. coli ribonucleic acid polymerases recognized the same lambda prom...
متن کاملMechanism of activation of cAMP-dependent protein kinase: in Mucor rouxii the apparent specific activity of the cAMP-activated holoenzyme is different than that of its free catalytic subunit.
Kinetic constants for peptide phosphorylation by the catalytic subunit of the dimorphic fungus Mucor rouxii protein kinase A were determined using 13 peptides derived from the peptide containing the basic consensus sequence RRASVA, plus kemptide, S6 peptide, and protamine. As a whole, although with a greater Km, the order of preference of the peptides by the M. rouxii catalytic subunit was simi...
متن کاملControl of dimorphism in Mucor by hexoses: inhibition of hyphal morphogenesis.
In anaerobic cultures of Mucor rouxii, morphogenesis was strongly dependent on hexose concentration as well as pCO(2). At low levels of hexose or CO(2), or both, hyphal development occurred; at high levels, the fungus developed as yeast cells. Other dimorphic strains of Mucor responded similarly to hexose and CO(2) but differred in their relative sensitivity to these agents. Glucose was the mos...
متن کاملLomofungin, an inhibitor of deoxyribonucleic acid-dependent ribonucleic acid polymerases.
Lomofungin, an antibiotic active against fungi, yeasts, and bacteria, was found to be a potent inhibitor of purified Escherichia coli deoxyribonucleic acid (DNA)-dependent ribonucleic acid (RNA) polymerase. It prevents RNA synthesis by a direct interaction with the polymerase and not with the template or substrate; chain elongation is halted promptly. Three DNA-dependent RNA polymerases isolate...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- The Journal of biological chemistry
دوره 250 2 شماره
صفحات -
تاریخ انتشار 1975