Search Results - "Kraal, B"

ssgA is essential for sporulation of Streptomyces coelicolor A3(2) and affects hyphal development by stimulating septum formation by van Wezel, G P, van der Meulen, J, Kawamoto, S, Luiten, R G, Koerten, H K, Kraal, B

“…The role of ssgA in cell division and development of streptomycetes was analyzed. An ssgA null mutant of Streptomyces coelicolor produced aerial hyphae but…”
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Identification of Novel RNA-Protein Contact in Complex of Ribosomal Protein S7 and 3'-Terminal Fragment of 16S rRNA in E. coli by Golovin, A V, Khayrullina, G A, Kraal, B, Kopylov, Capital A Cyrillic М

“…For prokaryotes in vitro, 16S rRNA and 20 ribosomal proteins are capable of hierarchical self- assembly yielding a 30S ribosomal subunit. The self-assembly is…”
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Selection of random RNA fragments as method for searching for a site of regulation of translation of E. coli streptomycin mRNA by ribosomal protein S7 by Surdina, A. V., Rassokhin, T. I., Golovin, A. V., Spiridonova, V. A., Kraal, B., Kopylov, A. M.

“…In E. coli cells ribosomal small subunit biogenesis is regulated by RNA—protein interactions involving protein S7. S7 initiates the subunit assembly…”
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Specific Peptide-Activated Proteolytic Cleavage of Escherichia coli Elongation Factor Tu by Georgiou, T., Y.-T. N. Yu, Ekunwe, S., Buttner, M. J., A.-M. Zuurmond, Kraal, B., Kleanthous, C., Snyder, L.

“…Phage exclusion is a form of programmed cell death in prokaryotes in which death is triggered by infection with phage, a seemingly altruistic response that…”
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The G222D mutation in elongation factor Tu inhibits the codon‐induced conformational changes leading to GTPase activation on the ribosome by Vorstenbosch, E., Pape, T., Rodnina, M. V., Kraal, B., Wintermeyer, W.

“…Elongation factor Tu (EF‐Tu) from Escherichia coli carrying the mutation G222D is unable to hydrolyze GTP on the ribosome and to sustain polypeptide synthesis…”
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Translational regulation by modifications of the elongation factor Tu by KRAAL, B, LIPPMANN, C, KLEANTHOUS, C

“…EF-Tu from E. coli, one of the superfamily of GTPase switch proteins, plays a central role in the fast and accurate delivery of aminoacyl-tRNAs to the…”
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Quality control of the elongation step of protein synthesis by tmRNP by Wower, J, Wower, I K, Kraal, B, Zwieb, C W

“…Trans-translation is a quality-control process, activated upon premature termination of protein elongation, which recycles stalled ribosomes and degrades…”
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The structural and functional basis for the kirromycin resistance of mutant EF‐Tu species in Escherichia coli by Mesters, J.R., Zeef, L.A., Hilgenfeld, R., Graaf, J.M., Kraal, B., Bosch, L.

“…A structural and functional understanding of resistance to the antibiotic kirromycin in Escherichia coli has been sought in order to shed new light on the…”
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Growth phase-dependent transcription of the Streptomyces ramocissimus tuf1 gene occurs from two promoters by Tieleman, L N, van Wezel, G P, Bibb, M J, Kraal, B

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Mutants of the elongation factor EF‐Tu, a new class of nonsense suppressors by Vijgenboom, E., Vink, T., Kraal, B., Bosch, L.

“…Read‐through of nonsense codons has been studied in wild‐type Escherichia coli cells and in cells harbouring mutant species of the elongation factor EF‐Tu. The…”
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Antibiotic resistance mechanisms of mutant EF-Tu species in Escherichia coli by Kraal, B, Zeef, L A, Mesters, J R, Boon, K, Vorstenbosch, E L, Bosch, L, Anborgh, P H, Parmeggiani, A, Hilgenfeld, R

“…Analysis of antibiotic-resistant EF-Tu mutants has revealed a connection between resistance and structural elements that participate in the GTPase switching…”
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Amino acid analysis of alfalfa mosaic virus coat proteins: an aid for viral strain identification by Kraal, B

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GTPase Center of Elongation Factor Tu is Activated by Occupation of the Second tRNA Binding Site by Van Noort, Johannes M., Kraal, Barend, Bosch, Leendert

“…Interaction of the elongation factor EF-Tu with the antibiotic kirromycin results in activation of the GTPase center of the factor and in induction of an…”
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Cross-linking of tRNA at two different sites of the elongation factor Tu by Van Noort, J M, Kraal, B, Bosch, L, La Cour, T F, Nyborg, J, Clark, B F

“…Recently, we reported on the induction by kirromycin of two tRNA binding sites on elongation factor Tu. To obtain independent information on the existence of…”
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A Second tRNA Binding Site on Elongation Factor Tu is Induced While the Factor is Bound to the Ribosome by Van Noort, Johannes M., Kraal, Barend, Bosch, Leendert

“…Previously, we reported that the antibiotic kirromycin induces two tRNA-binding sites on the elongation factor Tu. The classical binding site (site I) binds…”
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Kinetic Parameters for tmRNA Binding to Alanyl-tRNA Synthetase and Elongation Factor Tu from Escherichia coli by Barends, Sharief, Wower, Jacek, Kraal, Barend

“…Aminoacylation and transportation of tmRNA to stalled ribosomes constitute prerequisite steps for trans-translation, a process facilitating the release of…”
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Entrapping Ribosomes for Viral Translation: tRNA Mimicry as a Molecular Trojan Horse by Barends, Sharief, Bink, Hugo H.J., van den Worm, Sjoerd H.E., Pleij, Cornelis W.A., Kraal, Barend

“…Turnip yellow mosaic virus (TYMV) has a genomic plus-strand RNA with a 5′ cap followed by overlapping and different reading frames for the movement protein and…”
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The Streptomyces coelicolor ssgB gene is required for early stages of sporulation by Keijser, Bart J.F, Noens, Elke E.E, Kraal, Barend, Koerten, Henk K, van Wezel, Gilles P

“…ssgB was identified as a novel early sporulation gene in Streptomyces coelicolor. An ssgB deletion mutant failed to sporulate, over-produced actinorhodin, and…”
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tRNA-Like Structure Regulates Translation of Brome Mosaic Virus RNA by BARENDS, Sharief, RUDINGER-THIRION, Joëlle, FLORENTZ, Catherine, GIEGE, Richard, PLEIJ, Cornelis W. A, KRAAL, Barend

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Specific alterations of the EF‐Tu polypeptide chain considered in the light of its three‐dimensional structure by Duisterwinkel, F.J., Kraal, B., De Graaf, J.M., Talens, A., Bosch, L., Swart, G.W., Parmeggiani, A., La Cour, T.F., Nyborg, J., Clark, B.F.

“…Specific alterations of the elongation factor Tu (EF‐Tu) polypeptide chain have been identified in a number of mutant species of this elongation factor. In two…”
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