scholarly journals Paediatric neurosurgical implications of a ribosomopathy: illustrative case and literature review

2021 ◽  
Author(s):  
Suzanne Murphy ◽  
Gabriella Grima ◽  
Kshitij Mankad ◽  
Kristian Aquilina
Keyword(s):  
Literature Review ◽  
Ribosomal Subunit ◽  
Mass Effect ◽  
Genetic Mutation ◽  
Illustrative Case ◽  
Large Ribosomal Subunit ◽  
Local Mass ◽  
Intracranial Calcifications ◽  
Different Ages ◽  
Cerebral Microangiopathy

AbstractRibosomopathies are rare, recently defined entities. One of these, Labrune syndrome, is recognisable radiologically by its distinctive triad of leukoencephalopathy, intracranial calcifications and cysts (LCC). These cysts may have neurosurgical implications at different ages because of their progressive expansion and local mass effect. The aetiology of LCC is related to a widespread cerebral microangiopathy and is due to a genetic mutation in SNORD118, responsible for stabilisation of the large ribosomal subunit during assembly.

scholarly journals High Resolution Structure of the Large Ribosomal Subunit from a Mesophilic Eubacterium

Cell ◽  
2001 ◽  
Vol 107 (5) ◽  
pp. 679-688 ◽  
Author(s):  
Joerg Harms ◽  
Frank Schluenzen ◽  
Raz Zarivach ◽  
Anat Bashan ◽  
Sharon Gat ◽  
...  
Keyword(s):  
High Resolution ◽  
Ribosomal Subunit ◽  
Large Ribosomal Subunit ◽  
High Resolution Structure ◽  
Resolution Structure

scholarly journals A single N1-methyladenosine on the large ribosomal subunit rRNA impacts locally its structure and the translation of key metabolic enzymes

2018 ◽  
Vol 8 (1) ◽  
Author(s):  
Sunny Sharma ◽  
Johannes David Hartmann ◽  
Peter Watzinger ◽  
Arvid Klepper ◽  
Christian Peifer ◽  
...  
Keyword(s):  
Ribosomal Subunit ◽  
Metabolic Enzymes ◽  
Large Ribosomal Subunit

scholarly journals The enigmatic ribosomal stalk

2018 ◽  
Vol 51 ◽  
Author(s):  
Anders Liljas ◽  
Suparna Sanyal
Keyword(s):  
Early Phase ◽  
Ribosomal Subunit ◽  
Structure And Function ◽  
Large Ribosomal Subunit ◽  
Translation Factors ◽  
Ribosomal Stalk ◽  
And Function ◽  
High Degree

Abstract The large ribosomal subunit has a distinct feature, the stalk, extending outside the ribosome. In bacteria it is called the L12 stalk. The base of the stalk is protein uL10 to which two or three dimers of proteins bL12 bind. In archea and eukarya P1 and P2 proteins constitute the stalk. All these extending proteins, that have a high degree of flexibility due to a hinge between their N- and C-terminal parts, are essential for proper functionalization of some of the translation factors. The role of the stalk proteins has remained enigmatic for decades but is gradually approaching an understanding. In this review we summarise the knowhow about the structure and function of the ribosomal stalk till date starting from the early phase of ribosome research.

scholarly journals Analysis of subunit folding contribution of three yeast large ribosomal subunit proteins required for stabilisation and processing of intermediate nuclear rRNA precursors.

2021 ◽  
Author(s):  
Philipp Milkereit ◽  
Gisela Pöll ◽  
Michael Pilsl ◽  
Joachim Griesenbeck ◽  
Herbert Tschochner
Keyword(s):  
Electron Microscopy ◽  
Ribosomal Proteins ◽  
Ribosomal Subunit ◽  
Protein Assembly ◽  
Functional Coupling ◽  
Large Ribosomal Subunit ◽  
Cryo Electron Microscopy ◽  
Intrinsic Quality ◽  
Domain Arrangement ◽  
The Stability

In yeast and human cells many of the ribosomal proteins (r-proteins) are required for the stabilisation and productive processing of rRNA precursors. Functional coupling of r-protein assembly with the stabilisation and maturation of subunit precursors potentially promotes the production of ribosomes with defined composition. To further decipher mechanisms of such an intrinsic quality control pathway we analysed here the contribution of three yeast large ribosomal subunit r-proteins for intermediate nuclear subunit folding steps. Structure models obtained from single particle cryo-electron microscopy analyses provided evidence for specific and hierarchic effects on the stable positioning and remodelling of large ribosomal subunit domains. Based on these structural and previous biochemical data we discuss possible mechanisms of r-protein dependent hierarchic domain arrangement and the resulting impact on the stability of misassembled subunits.

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