نتایج جستجو برای: H27

تعداد نتایج: 62  

Journal: :Biopolymers 2011
Meredith Newby Spano Nils G Walter

Helix (H)27 of 16S ribosomal (r)RNA from Escherichia coli was dubbed the "switch helix" when mutagenesis suggested that two alternative base pair registers may have distinct functional roles in the bacterial ribosome. Although more recent genetic analyses suggest that H27 conformational switching is not required for translation, previous solution studies demonstrated that the isolated E. coli H...

2013
Åsa Segerstolpe Sander Granneman Petra Björk Flavia de Lima Alves Juri Rappsilber Charlotta Andersson Martin Högbom David Tollervey Lars Wieslander

Ribosomal subunit biogenesis in eukaryotes is a complex multistep process. Mrd1 is an essential and conserved small (40S) ribosomal subunit synthesis factor that is required for early cleavages in the 35S pre-ribosomal RNA (rRNA). Yeast Mrd1 contains five RNA-binding domains (RBDs), all of which are necessary for optimal function of the protein. Proteomic data showed that Mrd1 is part of the ea...

Journal: :Biochemistry 2004
John A H Hoerter Meredith Newby Lambert Miguel J B Pereira Nils G Walter

The original interpretation of a series of genetic studies suggested that the highly conserved Escherichia coli 16S ribosomal RNA helix 27 (H27) adopts two alternative secondary structure motifs, the 885 and 888 conformations, during each cycle of amino acid incorporation. Recent crystallographic and genetic evidence has called this hypothesis into question. To ask whether a slippery sequence s...

Journal: :RNA 2005
Meredith Newby Lambert John A H Hoerter Miguel J B Pereira Nils G Walter

Helix (H)27 from Escherichia coli 16S ribosomal (r)RNA is centrally located within the small (30S) ribosomal subunit, immediately adjacent to the decoding center. Bacterial 30S subunit crystal structures depicting Mg(2+) binding sites resolve two magnesium ions within the vicinity of H27: one in the major groove of the G886-U911 wobble pair, and one within the GCAA tetraloop. Binding of such me...

Journal: :Journal of clinical microbiology 1985
R J Gross L V Thomas B Rowe

Thirty-two strains of Escherichia coli belonging to a new O group, O166, were examined. Twenty-one strains had the flagella antigen H27, five had the H15 antigen, five had the H7 antigen, and one was nonmotile. All the H27 strains and the nonmotile strain produced heat-stable enterotoxin but not heat-labile enterotoxin. All the H7 strains produced heat-labile enterotoxin but not heat-stable ent...

Journal: :Japanese journal of infectious diseases 2007
Tetsuya Harada Midori Hiroi Fumihiko Kawamori Aki Furusawa Katsuhiko Ohata Kanji Sugiyama Takashi Masuda

Enteroaggregative Escherichia coli (EAEC), which is identifined by a special characteristic “stacked brick” aggregative adherence to cultured human epithelial cells (1), has been associated with acute and persistent diarrhea in children, in food poisoning diarrhea outbreaks and in overseas travelers (2). In Japan, a massive food-borne outbreak of gastrointestinal illness caused by EAEC O untype...

2003
Gila Shazberg Moshe Wolk Herbert Schmidt Iancu Sechter Giora Gottesman Dan Miron

Enteroaggregative Escherichia coli (EAEC) is a newly diarrheagenic agent wherein several predominant serotypes are reported. We studied the association between those serotypes, as clonal indicators, and the trait of enteroaggregative adherence to host cells, tested by polymerase chain reaction. We also evaluated the clinical manifestations of infection in 17 hospitalized children by our most co...

Journal: :Applied and environmental microbiology 1986
W J Page P L Dale

Azotobacter vinelandii stimulated the growth of Agrobacterium tumefaciens H2, H23, H24, H27, and ATCC 15955 on media containing insoluble iron sources. The Azotobacter vinelandii siderophores appeared to promote Agrobacterium tumefaciens growth by solubilizing mineral iron, and the ferrisiderophores so formed then acted as iron sources for Agrobacterium tumefaciens. Agrobactin, the Agrobacteriu...

Journal: :Food Microbiology 2021

Nisin is an antimicrobial peptide that commonly used as a food preservative and capable of inhibiting the pathogen Listeria monocytogenes. However, nisin ineffective in controlling L. monocytogenes Queso Fresco (QF). To address challenge, this work, we synthetic biology strategies to create series A derivatives by substituting residues 27, 30, 31 32 with positively charged amino acids (H, K R)....

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