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Genomes and Genes | K D YoungSummaryAffiliation: University of North Dakota Country: USA Publications
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Bacterial shapeKevin D Young
Department of Microbiology and Immunology, University of North Dakota School of Medicine, Grand Forks 58202 9037, USA
Mol Microbiol 49:571-80. 2003....
FtsZ collaborates with penicillin binding proteins to generate bacterial cell shape in Escherichia coliArchana Varma
Department of Microbiology and Immunology, University of North Dakota School of Medicine and Health Sciences, Grand Forks, ND 58202, USA
J Bacteriol 186:6768-74. 2004....- The selective value of bacterial shapeKevin D Young
Department of Microbiology and Immunology, University of North Dakota School of Medicine, Grand Forks, ND 58202 9037, USA
Microbiol Mol Biol Rev 70:660-703. 2006..Just as we are beginning to answer how bacteria create their shapes, it seems reasonable and essential that we expand our efforts to understand why they do so... - Reforming L forms: they need part of a wall after all?Kevin D Young
Department of Microbiology and Immunology, University of North Dakota School of Medicine, Grand Forks, ND 58202, USA
J Bacteriol 189:6509-11. 2007 - Bacterial morphology: why have different shapes?Kevin D Young
Department of Microbiology and Immunology, University of North Dakota School of Medicine and Health Sciences, Grand Forks, ND 58202 9037, USA
Curr Opin Microbiol 10:596-600. 2007..In short, if a bacterium needs to eat, divide or survive, or if it needs to attach, move or differentiate, then it can benefit from adopting an appropriate shape... - Why spherical Escherichia coli dies: the inside storyKevin D Young
Mailing address: Department of Microbiology and Immunology, University of North Dakota School of Medicine, Grand Forks, ND 58202, USA
J Bacteriol 190:1497-8. 2008 - Approaching the physiological functions of penicillin-binding proteins in Escherichia coliK D Young
Department of Microbiology and Immunology, School of Medicine and Health Sciences, University of North Dakota, Grand Forks 58202 9037, USA
Biochimie 83:99-102. 2001.... - Escherichia coli mutants lacking all possible combinations of eight penicillin binding proteins: viability, characteristics, and implications for peptidoglycan synthesisS A Denome
Department of Microbiology and Immunology, School of Medicine, University of North Dakota, Grand Forks, North Dakota 58202 9037, USA
J Bacteriol 181:3981-93. 1999..In addition, members of the set of PBP mutants will provide excellent starting points for answering fundamental questions about other aspects of cell wall metabolism... - AmpC and AmpH, proteins related to the class C beta-lactamases, bind penicillin and contribute to the normal morphology of Escherichia coliT A Henderson
Department of Microbiology and Immunology, School of Medicine, University of North Dakota, Grand Forks 58202 9037, USA
J Bacteriol 179:6112-21. 1997..These traits suggest that AmpC and AmpH may play roles in the normal course of peptidoglycan synthesis, remodeling, or recycling... - Separation of Escherichia coli penicillin-binding proteins into different membrane vesicles by agarose electrophoresis and sizing chromatographyM J Leidenix
Department of Microbiology and Immunology, University of North Dakota School of Medicine, Grand Forks 58202
J Bacteriol 171:5680-6. 1989..coli which is not observed when membrane vesicles are separated solely on the basis of density in sucrose gradients... - Reconstruction of Escherichia coli mrcA (PBP 1a) mutants lacking multiple combinations of penicillin binding proteinsB M Meberg
Department of Microbiology and Immunology, University of North Dakota School of Medicine, Grand Forks, North Dakota 58202 9037, USA
J Bacteriol 183:6148-9. 2001.... - Contributions of PBP 5 and DD-carboxypeptidase penicillin binding proteins to maintenance of cell shape in Escherichia coliD E Nelson
Department of Microbiology and Immunology, University of North Dakota School of Medicine and Health Sciences, Grand Forks, ND 58202 9037, USA
J Bacteriol 183:3055-64. 2001..coli... - Unequal distribution of penicillin-binding proteins among inner membrane vesicles of Escherichia coliG H Jacoby
Department of Microbiology and Immunology, University of North Dakota School of Medicine, Grand Forks 58202
J Bacteriol 170:3660-7. 1988..In addition, in cell lysates and in vesicle fractions, a 60,000-dalton aztreonam-insensitive PBP or protein fragment was observed which could potentially be confused with PBP3... - Lysis of Escherichia coli by beta-lactams which bind penicillin-binding proteins 1a and 1b: inhibition by heat shock proteinsJ K Powell
Department of Microbiology and Immunology, University of North Dakota School of Medicine, Grand Forks 58202
J Bacteriol 173:4021-6. 1991..Since many environmental stresses promote the expression of HSPs, it is possible that their presence contributes an additional mechanism toward development in bacteria of phenotypic tolerance to beta-lactam antibiotics... - Penicillin binding protein 5 affects cell diameter, contour, and morphology of Escherichia coliD E Nelson
Department of Microbiology and Immunology, School of Medicine, University of North Dakota, Grand Forks, North Dakota 58202 9037, USA
J Bacteriol 182:1714-21. 2000..We conclude that among the low-molecular-weight PBPs, PBP 5 plays a principle role in determining cell diameter, surface uniformity, and overall topology of the peptidoglycan sacculus... - Artifactual processing of penicillin-binding proteins 7 and 1b by the OmpT protease of Escherichia coliT A Henderson
Department of Microbiology and Immunology, School of Medicine, University of North Dakota, Grand Forks 58202 9001
J Bacteriol 176:256-9. 1994..The degradation of other PBPs during purification or storage may also be effected by OmpT... - Identification and cloning of the gene encoding penicillin-binding protein 7 of Escherichia coliT A Henderson
Department of Microbiology and Immunology, School of Medicine, University of North Dakota, Grand Forks 58202 9037, USA
J Bacteriol 177:2074-9. 1995..coli. No obvious growth defects were observed, suggesting that PBP 7 is not essential for growth under normal laboratory conditions... - Contribution of membrane-binding and enzymatic domains of penicillin binding protein 5 to maintenance of uniform cellular morphology of Escherichia coliDavid E Nelson
Department of Microbiology and Immunology, University of North Dakota School of Medicine, Grand Forks, North Dakota 58202 9037, USA
J Bacteriol 184:3630-9. 2002.... - Cell cycle-independent lysis of Escherichia coli by cefsulodin, an inhibitor of penicillin-binding proteins 1a and 1bG H Jacoby
Department of Microbiology and Immunology, University of North Dakota School of Medicine, Grand Forks 58202
J Bacteriol 173:1-5. 1991..Thus, cefsulodin-induced lysis is not linked to septation or to any other cell cycle-related event... - Sequences near the active site in chimeric penicillin binding proteins 5 and 6 affect uniform morphology of Escherichia coliAnindya S Ghosh
Department of Microbiology and Immunology, University of North Dakota School of Medicine, Grand Forks, North Dakota 58202 9037, USA
J Bacteriol 185:2178-86. 2003..coli PBP 5... - The Min system as a general cell geometry detection mechanism: branch lengths in Y-shaped Escherichia coli cells affect Min oscillation patterns and division dynamicsArchana Varma
Department of Microbiology and Immunology, University of North Dakota School of Medicine and Health Sciences, Grand Forks, ND 58202, USA
J Bacteriol 190:2106-17. 2008..The results provide further evidence that Min protein oscillations act as a general cell geometry detection mechanism that can locate poles even in branched cells... - In Escherichia coli, MreB and FtsZ direct the synthesis of lateral cell wall via independent pathways that require PBP 2Archana Varma
Department of Microbiology and Immunology, University of North Dakota School of Medicine and Health Sciences, Grand Forks, North Dakota 58202 9037, USA
J Bacteriol 191:3526-33. 2009..However, cell shape was determined only by the presence or absence of MreB and not by the even distribution of new wall material as directed by FtsZ... - Comparison of high-performance liquid chromatography and fluorophore-assisted carbohydrate electrophoresis methods for analyzing peptidoglycan composition of Escherichia coliShi Yan Li
Department of Microbiology and Immunology, University of North Dakota School of Medicine, Grand Forks, ND 58202 9037, USA
Anal Biochem 326:1-12. 2004..coli, and the use of FACE as an in vitro enzyme assay detected possible substrate preferences for the endopeptidase penicillin binding protein 4... - Sequence divergence of the murB and rrfB genes from Escherichia coli and Salmonella typhimuriumP M Dombrosky
Department of Microbiology and Immunology, School of Medicine, University of North Dakota, Grand Forks 58202 9001
Arch Microbiol 161:501-7. 1994..Thus, murB is an exception to the general observation that genes near the origin of replication show less divergence than do genes elsewhere in the bacterial chromosome... - Endopeptidase penicillin-binding proteins 4 and 7 play auxiliary roles in determining uniform morphology of Escherichia coliBernadette M Meberg
Department of Microbiology and Immunology, University of North Dakota School of Medicine, Grand Forks, ND 58202 9037, USA
J Bacteriol 186:8326-36. 2004.... - Metabolism of dibenzothiophene and naphthalene in Pseudomonas strains: complete DNA sequence of an upper naphthalene catabolic pathwayS A Denome
Department of Microbiology and Immunology, University of North Dakota School of Medicine, Grand Forks
J Bacteriol 175:6890-901. 1993..Our findings indicate that a single genetic pathway controls the metabolism of dibenzothiophene, naphthalene, and phenanthrene in strain C18 and that the DOX sequence encodes a complete upper naphthalene catabolic pathway similar to NAH... - FtsZ directs a second mode of peptidoglycan synthesis in Escherichia coliArchana Varma
Department of Microbiology and Immunology, University of North Dakota School of Medicine and Health Sciences, Grand Forks, ND 58202, USA
J Bacteriol 189:5692-704. 2007..In sum, the results indicate that in addition to nucleating cell septation in E. coli, FtsZ can direct the insertion of new peptidoglycan into portions of the lateral wall... - Daughter cell separation by penicillin-binding proteins and peptidoglycan amidases in Escherichia coliRicha Priyadarshini
Department of Microbiology and Immunology, University of North Dakota, Grand Forks, ND 58202 9037, USA
J Bacteriol 188:5345-55. 2006..Unexpectedly, amidase mutants lacking PBP 5 grew in long twisted chains instead of straight filaments, indicating that overall septal morphology was also defective in these strains... - Escherichia coli and other species of the Enterobacteriaceae encode a protein similar to the family of Mip-like FK506-binding proteinsS M Horne
Department of Microbiology and Immunology, School of Medicine, University of North Dakota, Grand Forks 58202 9037, USA
Arch Microbiol 163:357-65. 1995..Thus, mip-like genes are not found exclusively in bacteria having a predominately intracellular life style, but instead appear to be a new FKBP subfamily that is a common constituent of many bacteria... - Role of peptidoglycan amidases in the development and morphology of the division septum in Escherichia coliRicha Priyadarshini
Department of Microbiology and Immunology, University of North Dakota School of Medicine, Grand Forks, ND 58202 9037, USA
J Bacteriol 189:5334-47. 2007.... - Characterization of the desulfurization genes from Rhodococcus sp. strain IGTS8S A Denome
Department of Microbiology and Immunology, University of North Dakota School of Medicine, Grand Forks 58202
J Bacteriol 176:6707-16. 1994..The sox genes are plasmidborne and appear to be expressed as an operon in Rhodococcus sp. strain IGTS8 and in E. coli... - Bacterial shape: two-dimensional questions and possibilitiesKevin D Young
Department of Microbiology and Immunology, University of Arkansas for Medical Sciences, Little Rock, Arkansas 72205 7199, USA
Annu Rev Microbiol 64:223-40. 2010..In addition, surprising new observations show that the bacterial cell wall is more highly malleable than previously believed and that cells can alter and restore their shapes by relying only on internal mechanisms... - A simple gel electrophoretic method for analyzing the muropeptide composition of bacterial peptidoglycanK D Young
Department of Microbiology and Immunology, School of Medicine, University of North Dakota, Grand Forks, North Dakota 58202 9037, USA
J Bacteriol 178:3962-6. 1996..Thus, FACE may be used to identify interesting peptidoglycan samples prior to more-extensive analysis by HPLC, or FACE may eventually replace HPLC for some applications... - Septal and lateral wall localization of PBP5, the major D,D-carboxypeptidase of Escherichia coli, requires substrate recognition and membrane attachmentLakshmiprasad Potluri
Department of Microbiology and Immunology, University of Arkansas for Medical Sciences, Little Rock, AR 72205 7199, USA
Mol Microbiol 77:300-23. 2010..The results indicate that PBP5 localization to sites of ongoing peptidoglycan synthesis is substrate dependent and requires membrane attachment... - Helical disposition of proteins and lipopolysaccharide in the outer membrane of Escherichia coliAnindya S Ghosh
Department of Microbiology and Immunology, University of North Dakota School of Medicine and Health Sciences, Grand Forks, ND 58202-9037, USA
J Bacteriol 187:1913-22. 2005..coli has a defined in vivo organization in which a subfraction of proteins and LPS are embedded in stable domains at the poles and along one or more helical ribbons that span the length of this gram-negative rod... - beta-Lactam induction of colanic acid gene expression in Escherichia coliFrances C Sailer
Department of Microbiology and Immunology, University of North Dakota School of Medicine, Grand Forks, ND 58202-9037, USA
FEMS Microbiol Lett 226:245-9. 2003..Because colanic acid is important for maturation of biofilm architecture, antibiotics that increase its synthesis might exacerbate the formation or persistence of biofilms... - Loss of O-antigen increases cell shape abnormalities in penicillin-binding protein mutants of Escherichia coliAnindya S Ghosh
Department of Biotechnology, Indian Institute of Technology, Kharagpur, WB, India
FEMS Microbiol Lett 263:252-7. 2006..Thus, the O-antigen contributes to cell shape in E. coli, perhaps by reducing the number of ectopic poles, which may be the proximal cause of shape abnormalities... - Branching of Escherichia coli cells arises from multiple sites of inert peptidoglycanMiguel A de Pedro
Centro de Biologia Molecular Severo Ochoa, Consejo Superior de Investigaciones Cientificas, Universidad Autonoma de Madrid, Campus de Cantoblanco, 28049 Madrid, Spain
J Bacteriol 185:1147-52. 2003..These observations suggest that in dacA mutants, branches and other morphological anomalies may arise from split polar caps or by de novo generation of new poles built around inert peptidoglycan patches in the side walls of the cell... - Too many strictures on structureKevin D Young
Trends Microbiol 14:155-6. 2006.... - Role of penicillin-binding proteins in bacterial cell morphogenesisDavid L Popham
Department of Biology, Virginia Tech, Blacksburg, VA 24061, USA
Curr Opin Microbiol 6:594-9. 2003..In addition, the low molecular weight PBPs, by varying the substrates on which other PBPs act, alter peptidoglycan synthesis or turnover, with profound effects on morphology... - Branching sites and morphological abnormalities behave as ectopic poles in shape-defective Escherichia coliTrine Nilsen
Infectious Disease Division, Massachusetts General Hospital/Harvard Medical School, Boston, MA 02114, USA
Mol Microbiol 52:1045-54. 2004..Such mutants may help to unravel how particular proteins are targeted to bacterial poles, thereby creating important biochemical and functional asymmetries... - Common beta-lactamases inhibit bacterial biofilm formationClaude V Gallant
Department of Surgery, University of Toronto, Toronto, ON, Canada
Mol Microbiol 58:1012-24. 2005..Beta-lactamases likely affect PG remodelling, manifesting as perturbation of structures involved in bacterial adhesion that are required to initiate biofilm formation...