نتایج جستجو برای: l11

تعداد نتایج: 680  

Journal: :Journal of bacteriology 2001
X Yang E E Ishiguro

Amino acid-deprived rplK (previously known as relC) mutants of Escherichia coli cannot activate (p)ppGpp synthetase I (RelA) and consequently exhibit relaxed phenotypes. The rplK gene encodes ribosomal protein L11, suggesting that L11 is involved in regulating the activity of RelA. To investigate the role of L11 in the stringent response, a derivative of rplK encoding L11 lacking the N-terminal...

2013
Manato Ebina Fuminori Tsuruta Megumi C. Katoh Yu Kigoshi Akie Someya Tomoki Chiba

Nucleolus is a dynamic structure that controls biogenesis of ribosomal RNA and senses cellular stresses. Nucleolus contains a number of proteins including ribosomal proteins that conduct cellular stresses to downstream signaling such as p53 pathway. Recently, it has been reported that modification by a ubiquitin-like molecule, Nedd8, regulates subnuclear localization of ribosomal protein L11. M...

Journal: :Cell cycle 2007
Mu-Shui Dai Rosalie Sears Hua Lu

Several ribosomal proteins including L11 have been shown to activate p53 by inhibiting oncoprotein MDM2, leading to inhibition of cell cycle progression. Our recent study showed that L11 also inhibits oncoprotein c-Myc. Overexpression of L11 inhibits c-Myc-induced transcription and cell proliferation, while reduction of endogenous L11 increases these c-Myc activities. Interestingly, L11 is a tr...

Journal: :The Journal of biological chemistry 2005
Sarae L Bausch Ekaterina Poliakova David E Draper

Ribosomal protein L11 has two domains: the C-terminal domain (L11-C76) binds rRNA, whereas the N-terminal domain (L11-NTD) may variously interact with elongation factor G, the antibiotic thiostrepton, and rRNA. To begin to quantitate these interactions, L11 from Bacillus stearothermophilus has been overexpressed and its properties compared with those of L11-C76 alone in a fluorescence assay for...

Journal: :Land 2023

The Grain-for-Green Project (GFGP), one of the largest ecological restoration projects in China, has made a significant contribution to carbon neutrality. However, quantitative climate change and driving forces sequestration retired farmlands remains unclear. To analyze dynamics their forces, GlobeLand30 databases were used identify from 2001 2020; addition, net primary productivity (NPP) ident...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 1986
J R Cole M Nomura

The physiological importance of translational regulation in controlling the synthesis of ribosomal proteins from the L11 ribosomal protein operon was determined for the classical regulatory phenomena of growth rate dependence and stringent control. Translational regulation of the L11 operon by ribosomal protein L1, the L11 operon-specific translational repressor protein, was abolished by introd...

2007
Hendrik R. A. Jonker Serge Ilin S. Kaspar Grimm Jens Wöhnert Harald Schwalbe

Ribosomal proteins are assumed to stabilize specific RNA structures and promote compact folding of the large rRNA. The conformational dynamics of the protein between the bound and unbound state play an important role in the binding process. We have studied those dynamical changes in detail for the highly conserved complex between the ribosomal protein L11 and the GTPase region of 23S rRNA. The ...

Journal: :The EMBO journal 2007
Mu-Shui Dai Hugh Arnold Xiao-Xin Sun Rosalie Sears Hua Lu

The c-Myc oncoprotein promotes cell growth by enhancing ribosomal biogenesis through upregulation of RNA polymerases I-, II-, and III-dependent transcription. Overexpression of c-Myc and aberrant ribosomal biogenesis leads to deregulated cell growth and tumorigenesis. Hence, c-Myc activity and ribosomal biogenesis must be regulated in cells. Here, we show that ribosomal protein L11, a component...

Journal: :The EMBO journal 2004
Krishna P Bhat Koji Itahana Aiwen Jin Yanping Zhang

The ribosomal protein L11 binds to and suppresses the E3 ligase function of HDM2, thus activating p53. Despite being abundant as a component of the 60S large ribosomal subunit, L11 does not induce p53 under normal growth conditions. In search of mechanisms controlling L11-HDM2 interaction, we found that the induction of p53 under growth inhibitory conditions, such as low dose of actinomycin D o...

Journal: :Journal of molecular biology 2007
Donghan Lee Joseph D Walsh Ping Yu Michelle A Markus Theodora Choli-Papadopoulou Charles D Schwieters Susan Krueger David E Draper Yun-Xing Wang

The L11 binding site is one of the most important functional sites in the ribosome. The N-terminal domain of L11 has been implicated as a "reversible switch" in facilitating the coordinated movements associated with EF-G-driven GTP hydrolysis. The reversible switch mechanism has been hypothesized to require conformational flexibility involving re-orientation and re-positioning of the two L11 do...

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