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Article: The RNA-Binding Function of Ribosomal Proteins and Ribosome Biogenesis Factors in Human Health and Disease.

Catalanotto, Caterina / Barbato, Christian / Cogoni, Carlo / Benelli, Dario

2023 Volume 11, Issue 11

Abstract: The ribosome is a macromolecular complex composed of RNA and proteins that interact through an integrated and interconnected network to preserve its ancient core activities. In this review, we emphasize the pivotal role played by RNA-binding proteins as ... ...

Abstract	The ribosome is a macromolecular complex composed of RNA and proteins that interact through an integrated and interconnected network to preserve its ancient core activities. In this review, we emphasize the pivotal role played by RNA-binding proteins as a driving force in the evolution of the current form of the ribosome, underscoring their importance in ensuring accurate protein synthesis. This category of proteins includes both ribosomal proteins and ribosome biogenesis factors. Impairment of their RNA-binding activity can also lead to ribosomopathies, which is a group of disorders characterized by defects in ribosome biogenesis that are detrimental to protein synthesis and cellular homeostasis. A comprehensive understanding of these intricate processes is essential for elucidating the mechanisms underlying the resulting diseases and advancing potential therapeutic interventions.
Language	English
Publishing date	2023-11-04
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2720867-9
ISSN	2227-9059
ISSN	2227-9059
DOI	10.3390/biomedicines11112969
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Article ; Online: Inhibition of Eukaryotic Translation Initiation Factor 5A (eIF5A) Hypusination Suppress p53 Translation and Alters the Association of eIF5A to the Ribosomes.

Martella, Marianna / Catalanotto, Caterina / Talora, Claudio / La Teana, Anna / Londei, Paola / Benelli, Dario

International journal of molecular sciences

2020 Volume 21, Issue 13

Abstract: The eukaryotic translation initiation factor 5A (eIF5A) is an essential protein for the viability of the cells whose proposed function is to prevent the stalling of the ribosomes during translation elongation. eIF5A activity requires a unique and ... ...

Abstract	The eukaryotic translation initiation factor 5A (eIF5A) is an essential protein for the viability of the cells whose proposed function is to prevent the stalling of the ribosomes during translation elongation. eIF5A activity requires a unique and functionally essential post-translational modification, the change of a lysine to hypusine. eIF5A is recognized as a promoter of cell proliferation, but it has also been suggested to induce apoptosis. To date, the precise molecular mechanism through which eIF5A affects these processes remains elusive. In the present study, we explored whether eIF5A is involved in controlling the stress-induced expression of the key cellular regulator p53. Our results show that treatment of HCT-116 colon cancer cells with the deoxyhypusine (DHS) inhibitor N1-guanyl-1,7-diamineheptane (GC7) caused both inhibition of eIF5A hypusination and a significant reduction of p53 expression in UV-treated cells, and that eIF5A controls p53 expression at the level of protein synthesis. Furthermore, we show that treatment with GC7 followed by UV-induced stress counteracts the pro-apoptotic process triggered by p53 up-regulation. More in general, the importance of eIF5A in the cellular stress response is illustrated by the finding that exposure to UV light promotes the binding of eIF5A to the ribosomes, whereas UV treatment complemented by the presence of GC7 inhibits such binding, allowing a decrease of de novo synthesis of p53 protein.
MeSH term(s)	Apoptosis ; Cell Proliferation ; Colonic Neoplasms/genetics ; Colonic Neoplasms/metabolism ; Colonic Neoplasms/pathology ; Gene Expression Regulation, Neoplastic ; Humans ; Lysine/analogs & derivatives ; Lysine/chemistry ; Peptide Initiation Factors/chemistry ; Peptide Initiation Factors/genetics ; Peptide Initiation Factors/metabolism ; Protein Biosynthesis ; Protein Processing, Post-Translational ; RNA-Binding Proteins/chemistry ; RNA-Binding Proteins/genetics ; RNA-Binding Proteins/metabolism ; Ribosomes/metabolism ; Tumor Cells, Cultured ; Tumor Suppressor Protein p53/genetics ; Tumor Suppressor Protein p53/metabolism ; Eukaryotic Translation Initiation Factor 5A
Chemical Substances	Peptide Initiation Factors ; RNA-Binding Proteins ; TP53 protein, human ; Tumor Suppressor Protein p53 ; hypusine (3874VXF092) ; Lysine (K3Z4F929H6)
Language	English
Publishing date	2020-06-27
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms21134583
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Article ; Online: Loss of ATP2C1 function promotes trafficking and degradation of NOTCH1: Implications for Hailey-Hailey disease.

Zonfrilli, Azzurra / Truglio, Federica / Simeone, Alessandra / Pelullo, Maria / De Turris, Valeria / Benelli, Dario / Checquolo, Saula / Bellavia, Diana / Palermo, Rocco / Uccelletti, Daniela / Screpanti, Isabella / Cialfi, Samantha / Talora, Claudio

Experimental dermatology

2023 Volume 32, Issue 6, Page(s) 787–798

Abstract: Hailey-Hailey disease (HHD) is a rare autosomal dominantly inherited disorder caused by mutations in the ATP2C1 gene that encodes an adenosine triphosphate (ATP)-powered calcium channel pump. HHD is characterized by impaired epidermal cell-to-cell ... ...

Abstract	Hailey-Hailey disease (HHD) is a rare autosomal dominantly inherited disorder caused by mutations in the ATP2C1 gene that encodes an adenosine triphosphate (ATP)-powered calcium channel pump. HHD is characterized by impaired epidermal cell-to-cell adhesion and defective keratinocyte growth/differentiation. The mechanism by which mutant ATP2C1 causes HHD is unknown and current treatments for affected individuals do not address the underlying defects and are ineffective. Notch signalling is a direct determinant of keratinocyte growth and differentiation. We found that loss of ATP2C1 leads to impaired Notch1 signalling, thus deregulation of the Notch signalling response is therefore likely to contribute to HHD manifestation. NOTCH1 is a transmembrane receptor and upon ligand binding, the intracellular domain (NICD) translocates to the nucleus activating its target genes. In the context of HHD, we found that loss of ATP2C1 function promotes upregulation of the active NOTCH1 protein (NICD-Val1744). Here, deeply exploring this aspect, we observed that NOTCH1 activation is not associated with the transcriptional enhancement of its targets. Moreover, in agreement with these results, we found a cytoplasmic localization of NICD-Val1744. We have also observed that ATP2C1-loss is associated with the degradation of NICD-Val1744 through the lysosomal/proteasome pathway. These results show that ATP2C1-loss could promote a mechanism by which NOTCH1 is endocytosed and degraded by the cell membrane. The deregulation of this phenomenon, finely regulated in physiological conditions, could in HHD lead to the deregulation of NOTCH1 with alteration of skin homeostasis and disease manifestation.
MeSH term(s)	Humans ; Pemphigus, Benign Familial/genetics ; Pemphigus, Benign Familial/metabolism ; Skin/metabolism ; Keratinocytes/metabolism ; Mutation ; Epidermis/metabolism ; Calcium-Transporting ATPases/genetics ; Calcium-Transporting ATPases/metabolism ; Receptor, Notch1/genetics ; Receptor, Notch1/metabolism
Chemical Substances	Calcium-Transporting ATPases (EC 7.2.2.10) ; NOTCH1 protein, human ; Receptor, Notch1 ; ATP2C1 protein, human (EC 7.2.2.10)
Language	English
Publishing date	2023-02-23
Publishing country	Denmark
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1130936-2
ISSN	1600-0625 ; 0906-6705
ISSN (online)	1600-0625
ISSN	0906-6705
DOI	10.1111/exd.14769
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Article: The Archaeal Elongation Factor EF-2 Induces the Release of aIF6 From 50S Ribosomal Subunit.

Lo Gullo, Giada / De Santis, Maria Luisa / Paiardini, Alessandro / Rosignoli, Serena / Romagnoli, Alice / La Teana, Anna / Londei, Paola / Benelli, Dario

Frontiers in microbiology

2021 Volume 12, Page(s) 631297

Abstract: The translation factor IF6 is a protein of about 25 kDa shared by the Archaea and the Eukarya but absent in Bacteria. It acts as a ribosome anti-association factor that binds to the large subunit preventing the joining to the small subunit. It must be ... ...

Abstract	The translation factor IF6 is a protein of about 25 kDa shared by the Archaea and the Eukarya but absent in Bacteria. It acts as a ribosome anti-association factor that binds to the large subunit preventing the joining to the small subunit. It must be released from the large ribosomal subunit to permit its entry to the translation cycle. In Eukarya, this process occurs by the coordinated action of the GTPase Efl1 and the docking protein SBDS. Archaea do not possess a homolog of the former factor while they have a homolog of SBDS. In the past, we have determined the function and ribosomal localization of the archaeal (
Language	English
Publishing date	2021-03-24
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2587354-4
ISSN	1664-302X
ISSN	1664-302X
DOI	10.3389/fmicb.2021.631297
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Article ; Online: Optimization of an In Vitro Transcription/Translation System Based on

Lo Gullo, Giada / Mattossovich, Rosanna / Perugino, Giuseppe / La Teana, Anna / Londei, Paola / Benelli, Dario

Archaea (Vancouver, B.C.)

2019 Volume 2019, Page(s) 9848253

Abstract: A system is described which permits the efficient synthesis of ... ...

Abstract	A system is described which permits the efficient synthesis of proteins
MeSH term(s)	Cell-Free System ; Complex Mixtures/metabolism ; DNA, Archaeal/genetics ; Hot Temperature ; Promoter Regions, Genetic ; Protein Biosynthesis ; RNA, Messenger/metabolism ; RNA, Ribosomal, 16S/genetics ; RNA, Ribosomal, 23S/genetics ; Sulfolobus solfataricus/enzymology ; Transcription, Genetic
Chemical Substances	Complex Mixtures ; DNA, Archaeal ; RNA, Messenger ; RNA, Ribosomal, 16S ; RNA, Ribosomal, 23S
Language	English
Publishing date	2019-02-11
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1472-3654
ISSN (online)	1472-3654
DOI	10.1155/2019/9848253
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Article ; Online: Translation initiation in Archaea: conserved and domain-specific features.

Benelli, Dario / Londei, Paola

Biochemical Society transactions

2011 Volume 39, Issue 1, Page(s) 89–93

Abstract: Initiation is a critical step in translation, during which the ribosome lands on the start codon and sets the correct reading frame for mRNA decoding. The rate and efficiency of translation are largely determined by initiation, which is therefore the ... ...

Abstract	Initiation is a critical step in translation, during which the ribosome lands on the start codon and sets the correct reading frame for mRNA decoding. The rate and efficiency of translation are largely determined by initiation, which is therefore the preferred target of translation regulation mechanisms. Initiation has incurred an extensive evolutionary divergence among the primary domains of cell descent. The Archaea, albeit prokaryotes, have an initiation mechanism and apparatus more complex than those of the Bacteria; the molecular details of archaeal initiation are just beginning to be unravelled. The most notable aspects of archaeal initiation are the presence of two, perhaps three, distinct mechanisms for mRNA-ribosome interaction and the presence of a relatively large set of IFs (initiation factors), several of which are shared exclusively with the Eukarya. Among these, the protein termed a/eIF2 (archaeal/eukaryotic IF2) and aIF6 (archaeal IF6) are of special interest, since they appear to play key regulatory roles in the Eukarya. Studies of the function of these factors in Archaea have uncovered new features that will help to elucidate their conserved and domain-specific functions.
MeSH term(s)	Archaea/genetics ; Archaea/metabolism ; Archaeal Proteins/chemistry ; Archaeal Proteins/genetics ; Archaeal Proteins/metabolism ; Bacterial Proteins/chemistry ; Bacterial Proteins/metabolism ; Eukaryotic Initiation Factor-2/genetics ; Eukaryotic Initiation Factor-2/metabolism ; Models, Molecular ; Nucleic Acid Conformation ; Peptide Initiation Factors/chemistry ; Peptide Initiation Factors/genetics ; Peptide Initiation Factors/metabolism ; Protein Biosynthesis ; Protein Conformation ; Protein Subunits/chemistry ; Protein Subunits/metabolism ; RNA, Messenger/chemistry ; RNA, Messenger/metabolism ; Ribosomes/metabolism
Chemical Substances	Archaeal Proteins ; Bacterial Proteins ; Eukaryotic Initiation Factor-2 ; Peptide Initiation Factors ; Protein Subunits ; RNA, Messenger
Language	English
Publishing date	2011-01
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	184237-7
ISSN	1470-8752 ; 0300-5127
ISSN (online)	1470-8752
ISSN	0300-5127
DOI	10.1042/BST0390089
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Article ; Online: Begin at the beginning: evolution of translational initiation.

Benelli, Dario / Londei, Paola

Research in microbiology

2009 Volume 160, Issue 7, Page(s) 493–501

Abstract: Initiation of protein synthesis, entailing ribosomal recognition of the mRNA start codon and setting of the correct reading frame, is the rate-limiting step in translation and the main target of translation regulation in all modern cells. As efficient ... ...

Abstract	Initiation of protein synthesis, entailing ribosomal recognition of the mRNA start codon and setting of the correct reading frame, is the rate-limiting step in translation and the main target of translation regulation in all modern cells. As efficient selection of the translation start site is vital for survival of extant cells, a mechanism for ensuring this may already have been in existence in the last universal common ancestor of present-day cells. This article reviews known features of the molecular machinery for initiation in the primary domains of life, Bacteria, Archaea and Eukarya, and attempts to identify conserved features that may be useful for reconstructing a model of the ancestral initiation apparatus.
MeSH term(s)	Archaea/physiology ; Bacterial Physiological Phenomena ; Eukaryota/physiology ; Evolution, Molecular ; Models, Biological ; Models, Molecular ; Peptide Chain Initiation, Translational
Language	English
Publishing date	2009-09
Publishing country	France
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	1004220-9
ISSN	1769-7123 ; 0923-2508
ISSN (online)	1769-7123
ISSN	0923-2508
DOI	10.1016/j.resmic.2009.06.003
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Article ; Online: Optimization of an in Vitro Transcription/Translation System Based on Sulfolobus solfataricus Cell Lysate

Lo Gullo, Giada / Mattossovich, Rosanna / Perugino, Giuseppe / La Teana, Anna / Londei, Paola / Benelli, Dario

2019

Keywords	Microbiology ; Physiology ; Ecology ; Evolution ; Behavior and Systematics
Language	English
Publishing country	it
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article: In vitro studies of archaeal translational initiation.

Benelli, Dario / Londei, Paola

Methods in enzymology

2007 Volume 430, Page(s) 79–109

Abstract: Initiation is the step of translation that has incurred the greatest evolutionary divergence. In silico and experimental studies have shown that archaeal translation initiation resembles neither the bacterial nor the eukaryotic paradigm, but shares ... ...

Abstract	Initiation is the step of translation that has incurred the greatest evolutionary divergence. In silico and experimental studies have shown that archaeal translation initiation resembles neither the bacterial nor the eukaryotic paradigm, but shares features with both. The structure of mRNA in archaea is similar to the bacterial one, although the protein factors that assist translational initiation are more numerous than in bacteria and are homologous to eukaryotic proteins. This chapter describes a number of techniques that can be used for in vitro studies of archaeal translation and translational initiation, using as a model system the thermophilic crenarcheon Sulfolobus solfataricus, growing optimally at about 80 degrees in an acidic environment.
MeSH term(s)	Archaeal Proteins/genetics ; Archaeal Proteins/metabolism ; Macromolecular Substances ; Methionine/metabolism ; Peptide Initiation Factors/isolation & purification ; Peptide Initiation Factors/metabolism ; Protein Biosynthesis ; RNA, Archaeal/metabolism ; RNA, Messenger/metabolism ; RNA, Transfer/isolation & purification ; RNA, Transfer/metabolism ; RNA, Transfer, Met/isolation & purification ; RNA, Transfer, Met/metabolism ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism ; Ribosomes/chemistry ; Ribosomes/metabolism ; Sulfolobus solfataricus/genetics ; Sulfolobus solfataricus/metabolism
Chemical Substances	Archaeal Proteins ; Macromolecular Substances ; Peptide Initiation Factors ; RNA, Archaeal ; RNA, Messenger ; RNA, Transfer, Met ; Recombinant Proteins ; RNA, Transfer (9014-25-9) ; Methionine (AE28F7PNPL)
Language	English
Publishing date	2007
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	0076-6879
ISSN	0076-6879
DOI	10.1016/S0076-6879(07)30005-0
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Article ; Online: Translation initiation in the crenarchaeon Sulfolobus solfataricus: eukaryotic features but bacterial route.

La Teana, Anna / Benelli, Dario / Londei, Paola / Bläsi, Udo

Biochemical Society transactions

2013 Volume 41, Issue 1, Page(s) 350–355

Abstract: The formation of the translation initiation complex represents the rate-limiting step in protein synthesis. Translation initiation in the crenarchaeon Sulfolobus solfataricus depends on several translation IFs (initiation factors), some of which have ... ...

Abstract	The formation of the translation initiation complex represents the rate-limiting step in protein synthesis. Translation initiation in the crenarchaeon Sulfolobus solfataricus depends on several translation IFs (initiation factors), some of which have eukaryal but no bacterial counterparts. In the present paper, we review the current knowledge of the structure, function and evolution of the IFs in S. solfataricus in the context of eukaryotic and bacterial orthologues. Despite similarities between eukaryotic and S. solfataricus IFs, the sequence of events in translation initiation in S. solfataricus follows the bacterial mode.
MeSH term(s)	Evolution, Molecular ; Peptide Initiation Factors/genetics ; Protein Biosynthesis ; Sulfolobus solfataricus/genetics
Chemical Substances	Peptide Initiation Factors
Language	English
Publishing date	2013-01-23
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	184237-7
ISSN	1470-8752 ; 0300-5127
ISSN (online)	1470-8752
ISSN	0300-5127
DOI	10.1042/BST20120300
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