Protein Synthesis During Morphogenesis of Mucor racemosusOrlowski, Michael; Sypherd, Paul S.
doi: N/Apmid: 914775
Cells of Mucor racemosus were labeled with L - 14 Cleucine during the yeast-to-hyphae morphogenesis that follows a change of atmosphere from CO 2 to air. Pulse-labeling kinetics and the steady-state accumulation of incorporated L - 14 Cleucine were determined throughout the period of cellular differentiation. We determined that the L - 14 Cleucine was taken up by all forms of the organism, was not altered from the form of L -leucine, and was incorporated exclusively into protein. The intracellular pool of free L -leucine was small in comparison with those of the other L -amino acids, remained relatively constant in size during morphogenesis, and was rapidly equilibrated with exogenous leucine. Approximately the same internal radiospecific activities were attained throughout development shortly after addition of L - 14 Cleucine to a culture. Experiments performed with leucine auxotrophs suggested that endogenous synthesis of leucine in prototrophs does not affect the measured rates of incorporation. Experiments performed with 14 C-labeled L -isoleucine, L -proline, L -lysine, and L -arginine produced results qualitatively the same as with L -leucine. The accumulation of incorporated L - 14 Cleucine in a culture of M. racemosus undergoing the air-induced yeast-to-hyphae transition reflected the change in growth rate that accompanied the morphogenesis. However, the specific rate of protein synthesis measured throughout the developmental process displayed a characteristic acceleration during the emergence of germ tubes which was followed by a decline when all further growth took the form of hyphal elongation. Data are presented suggesting that this response is a correlate of morphogenesis rather than a consequence of the atmospheric change per se. J Bacteriol. 1977 October; 132(1): 209-218 Copyright © 1977 American Society for Microbiology . All Rights Reserved.
Role of methionine in the synthesis of nucleoside Q in Escherichia coli transfer ribonucleic acid.Katze, J R; Simonian, M H; Mosteller, R D
doi: N/Apmid: 334722
Previously, we reported that starvation of Rel Escherichia coli for methionine, but not leucine or histidine, results in chromatographically unique species of aspartyl-specific transfer ribonucleic acid (tRNAAsp) lacking the modified nucleoside Q. The present studies demonstrate that methionine starvation of Rel+ E. coli yields a qualitatively similar, but less pronounced, effect. Furthermore, during recovery from methionine starvation in Rel E. coli, the chromatographic elution pattern of tRNAAsp shifts towards that observed for unstarved cells after 1 h of recovery, and the shift appears complete after 2 h of recovery. This shift is inhibited by rifampin. Incorporation of 2-14Cmethionine or methyl-3Hmethionine into growing cells of E. coli does not result in labeling of nucleoside Q. We interpret these findings to indicate that methionine has an indirect role in Q formation and that Q-deficient tRNA can be modified slowly to contain Q but that transcription is required. The chromatographic elution patterns of tRNAAsp from Rel E. coli starved for arginine, lysine, or glutamic acid indicate that these amino acids are not the source of the three- or five-carbon sequences in the modified portion of Q. J Bacteriol. 1977 October; 132(1): 174-179
2-Hydroxypyridine Metabolism and Pigment Formation in Three Arthrobacter SpeciesKolenbrander, P. E.; Weinberger, M.
doi: N/Apmid: 199576
2-Hydroxypyridine Metabolism and Pigment Formation in Three Arthrobacter Species P. E. Kolenbrander and M. Weinberger † 1 Department of Microbiology and Cell Biology, The Pennsylvania State University, University Park, Pennsylvania 16802 ABSTRACT Three species of the genus Arthrobacter, A. crystallopoietes, A. pyridinolis, and A. viridescens , have the capabilities to utilize 2-hydroxypyridine (2-HP) as the sole source of carbon and nitrogen for growth and to produce an extracellular crystalline pigment from this substrate. Degradation of 2-HP by cell-free extracts requires the presence of both reduced nicotinamide adenine dinucleotide and molecular oxygen and is stimulated by flavin mononucleotide, suggesting the presence of a monooxygenase activity in the extract. Loss of the ability to produce pigment at a high spontaneous frequency, 0.26% loss per generation, is observed only with A. crystallopoietes and can be visualized by the presence of sectored and fully nonpigmented colonies on solid media containing 2-HP. Concomitant with the loss of pigment-producing character are both loss of ability to utilize 2-HP for growth and oxidation of 2-HP by cell-free extracts. These three 2-HP-associated characteristics also are lost simultaneously by treating cultures of A. crystallopoietes with curing agents, such as acridine orange and mitomycin C, but are not curable in A. pyridinolis or A. viridescens . All nonpigmented strains of A. crystallopoietes are nonrevertible for these properties. These data suggest that 2-HP-related characteristics are plasmid determined in A. crystallopoietes but not in A. pyridinolis and A. viridescens . A survey for the presence of plasmids in these three species and two physiologically unrelated species, A. globiformis and A. atrocyaneus , revealed plasmid material only in A. globiformis and A. crystallopoietes .
Physiological Effects of Growth of an Escherichia coli Temperature-Sensitive dnaZ Mutant at Nonpermissive TemperaturesChu, Herman; Malone, Margaret M.; Haldenwang, William G.; Walker, James R.
doi: N/Apmid: 334720
Physiological Effects of Growth of an Escherichia coli Temperature-Sensitive dnaZ Mutant at Nonpermissive Temperatures Herman Chu , Margaret M. Malone , William G. Haldenwang and James R. Walker 1 Department of Microbiology, The University of Texas at Austin, Austin, Texas 78712 ABSTRACT The physiological effects of incubation at nonpermissive temperatures of Escherichia coli mutants that carry a temperature-sensitive dnaZ allele ( dnaZ (Ts) 2016 ) were examined. The temperature at which the dnaZ (Ts) protein becomes inactivated in vivo was investigated by measurements of deoxyribonucleic acid (DNA) synthesis at temperatures intermediate between permissive and nonpermissive. DNA synthesis inhibition was reversible by reducing the temperature of cultures from 42 to 30°C; DNA synthesis resumed immediately after temperature reduction and occurred even in the presence of chloramphenicol. Inasmuch as DNA synthesis could be resumed in the absence of protein synthesis, we concluded that the protein product of the dnaZ allele (Ts) 2016 is renaturable. Cell division, also inhibited by 42°C incubation, resumed after temperature reduction, but the length of time required for resumption depended on the duration of the period at 42°C. Replicative synthesis of cellular DNA, examined in vitro in toluene-permeabilized cells, was temperature sensitive. Excision repair of ultraviolet light-induced DNA lesions was partially inhibited in dnaZ (Ts) cells at 42°C. The dnaZ + product participated in the synthesis of both Okazaki piece (8–12 S ) and high-molecular-weight DNA. During incubation of dnaZ (Ts)(λ) lysogens at 42°C, prophage induction occurred, and progeny phage were produced during subsequent incubation at 30°C. The temperature sensitivity of both DNA synthesis and cell division in the dnaZ (Ts) 2016 mutant was suppressed by high concentrations of sucrose, lactose, or NaCl. Incubation at 42°C was neither mutagenic nor antimutagenic for the dnaZ (Ts) mutant. Copyright © 1977 American Society for Microbiology CiteULike Connotea Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter What's this? « Previous | Next Article » Table of Contents This Article J. Bacteriol. October 1977 vol. 132 no. 1 151-158 » Abstract PDF Classifications Genetics and Molecular Biology Services Email this article to a colleague Similar articles in ASM journals Alert me when this article is cited Alert me if a correction is posted Similar articles in this journal Similar articles in Web of Science Similar articles in PubMed Alert me to new issues of JB Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Load citing article information Citing articles via Web of Science Citing articles via Google Scholar Google Scholar Articles by Chu, H. Articles by Walker, J. R. Search for related content PubMed PubMed citation Articles by Chu, H. Articles by Walker, J. R. Related Content Load related web page information Social Bookmarking CiteULike Connotea Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter What's this? current issue January 2012, volume 194, issue 1 Alert me to new issues of JB About JB Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy JB RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • [email protected] Print ISSN: 0021-9193 Online ISSN: 1098-5530 Copyright © 2011 by the American Society for Microbiology. For an alternate route to JB .asm.org, visit: http://intl- JB .asm.org | More Info»
Tryptophan-transducing bacteriophages: in vitro studies with restriction endonucleases HindII + III and Escherichia coli ribonucleic acid polymerase.Jones, B B; Reznikoff, W S
doi: N/Apmid: 334724
The HindII + III restriction enzyme fragmentation pattern of various lambda-phi80trp deoxyribonucleic acid molecules is presented. An analysis of deoxyribonucleic acid molecules carrying deletions ending within the trp regulatory elements and a deoxyribonucleic acid molecule carrying a deletion within trpE indicates that a fragment of 8.3 X 10(5) daltons contains at least part of the trp promoter, the entire trp leader region, and part of the trpE gene. The observation that ribonucleic acid polymerase, when present in the HindII + III digestion mixture, results in the fusion of this 8.3 X 10(5)-dalton fragment to the preceding bacterial fragment suggests that HindII + III cuts within trpP. J Bacteriol. 1977 October; 132(1): 270-281
Immunological study of the regulation of cellular arylsulfatase synthesis in Klebsiella aerogenes.Murooka, Y; Yamada, T; Tanabe, S; Harada, T
doi: N/Apmid: 72063
Immunological study of the regulation of cellular arylsulfatase synthesis in Klebsiella aerogenes. Y Murooka , T Yamada , S Tanabe and T Harada ABSTRACT Regulation of cellular arylsulfatase synthesis in Klebsiella aerogenes was analyzed by immunological techniques. Antibody directed against the purified arylsulfatase from K. aerogenes W70 was obtained from rabbits and characterized by immunoelectrophoresis, double-diffusion, quantitative precipitation, and enzyme neutralization tests. Arylsulfatase was located in the periplasmic space when the wild-type strain was cultured with methionine or with inorganic sulfate plus tyramine, but not with inorganic sulfate without tyramine, as the sole sulfur source. Tyramine oxidase was retained in the membrane fraction prepared from cells grown in the presence of tyramine. Arylsulfatase protein was not synthesized in the presence of tyramine and inorganic sulfate by mutant K611, which is deficient in tyramine oxidase (tynA). We conclude that the expression of the arylsulfatase gene (atsA) is regulated by the expression of tynA and that inorganic sulfate serves as a corepressor. In addition, strains mutated in the atsA gene were analyzed by using antibody. CiteULike Connotea Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter What's this? « Previous | Next Article » Table of Contents This Article J. Bacteriol. October 1977 vol. 132 no. 1 247-253 » Abstract PDF Classifications Research Article Services Email this article to a colleague Similar articles in ASM journals Alert me when this article is cited Alert me if a correction is posted Similar articles in this journal Similar articles in Web of Science Similar articles in PubMed Alert me to new issues of JB Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Load citing article information Citing articles via Web of Science Citing articles via Google Scholar Google Scholar Articles by Murooka, Y. Articles by Harada, T. Search for related content PubMed PubMed citation Articles by Murooka, Y. Articles by Harada, T. Related Content Load related web page information Social Bookmarking CiteULike Connotea Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter What's this? current issue January 2012, volume 194, issue 1 Alert me to new issues of JB About JB Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy JB RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • [email protected] Print ISSN: 0021-9193 Online ISSN: 1098-5530 Copyright © 2011 by the American Society for Microbiology. For an alternate route to JB .asm.org, visit: http://intl- JB .asm.org | More Info»
Protein Synthesis During Morphogenesis of Mucor racemosusOrlowski, Michael; Sypherd, Paul S.
doi: N/Apmid: 914775
Protein Synthesis During Morphogenesis of Mucor racemosus Michael Orlowski and Paul S. Sypherd 1 Department of Medical Microbiology, California College of Medicine, University of California, Irvine, California 92717 ABSTRACT Cells of Mucor racemosus were labeled with l -( 14 C)leucine during the yeast-to-hyphae morphogenesis that follows a change of atmosphere from CO 2 to air. Pulse-labeling kinetics and the steady-state accumulation of incorporated l -( 14 C)leucine were determined throughout the period of cellular differentiation. We determined that the l -( 14 C)leucine was taken up by all forms of the organism, was not altered from the form of l -leucine, and was incorporated exclusively into protein. The intracellular pool of free l -leucine was small in comparison with those of the other l -amino acids, remained relatively constant in size during morphogenesis, and was rapidly equilibrated with exogenous leucine. Approximately the same internal radiospecific activities were attained throughout development shortly after addition of l -( 14 C)leucine to a culture. Experiments performed with leucine auxotrophs suggested that endogenous synthesis of leucine in prototrophs does not affect the measured rates of incorporation. Experiments performed with 14 C-labeled l -isoleucine, l -proline, l -lysine, and l -arginine produced results qualitatively the same as with l -leucine. The accumulation of incorporated l -( 14 C)leucine in a culture of M. racemosus undergoing the air-induced yeast-to-hyphae transition reflected the change in growth rate that accompanied the morphogenesis. However, the specific rate of protein synthesis measured throughout the developmental process displayed a characteristic acceleration during the emergence of germ tubes which was followed by a decline when all further growth took the form of hyphal elongation. Data are presented suggesting that this response is a correlate of morphogenesis rather than a consequence of the atmospheric change per se. Copyright © 1977 American Society for Microbiology CiteULike Connotea Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter What's this? « Previous | Next Article » Table of Contents This Article J. Bacteriol. October 1977 vol. 132 no. 1 209-218 » Abstract PDF Classifications Physiology and Metabolism Services Email this article to a colleague Similar articles in ASM journals Alert me when this article is cited Alert me if a correction is posted Similar articles in this journal Similar articles in Web of Science Similar articles in PubMed Alert me to new issues of JB Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Load citing article information Citing articles via Web of Science Citing articles via Google Scholar Google Scholar Articles by Orlowski, M. Articles by Sypherd, P. S. Search for related content PubMed PubMed citation Articles by Orlowski, M. Articles by Sypherd, P. S. Related Content Load related web page information Social Bookmarking CiteULike Connotea Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter What's this? current issue January 2012, volume 194, issue 1 Alert me to new issues of JB About JB Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy JB RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • [email protected] Print ISSN: 0021-9193 Online ISSN: 1098-5530 Copyright © 2011 by the American Society for Microbiology. For an alternate route to JB .asm.org, visit: http://intl- JB .asm.org | More Info»