The P1/P2 Protein Heterodimers Assemble to the Ribosomal Stalk at the Moment When the Ribosome Is Committed to Translation but Not to the Native 60S Ribosomal Subunit in Saccharomyces cerevisiae

Biochemistry ◽  
2014 ◽  
Vol 53 (25) ◽  
pp. 4105-4112 ◽  
Author(s):  
A. Bautista-Santos ◽  
S. Zinker
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Ribosomal Subunit ◽  
Ribosomal Stalk ◽  
P2 Protein ◽  
The Moment

scholarly journals The Putative RNA Helicase Dbp6p Functionally Interacts With Rpl3p, Nop8p and the Novel trans-acting Factor Rsa3p During Biogenesis of 60S Ribosomal Subunits in Saccharomyces cerevisiae

Genetics ◽  
2004 ◽  
Vol 166 (4) ◽  
pp. 1687-1699
Author(s):  
Jesús de la Cruz ◽  
Thierry Lacombe ◽  
Olivier Deloche ◽  
Patrick Linder ◽  
Dieter Kressler
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Ribosome Biogenesis ◽  
Null Allele ◽  
Ribosomal Subunit ◽  
Interaction Network ◽  
The Novel ◽  
Rna Helicases ◽  
Ribosomal Subunits ◽  
Synthetic Lethal ◽  
Synthetically Lethal

Abstract Ribosome biogenesis requires at least 18 putative ATP-dependent RNA helicases in Saccharomyces cerevisiae. To explore the functional environment of one of these putative RNA helicases, Dbp6p, we have performed a synthetic lethal screen with dbp6 alleles. We have previously characterized the nonessential Rsa1p, whose null allele is synthetically lethal with dbp6 alleles. Here, we report on the characterization of the four remaining synthetic lethal mutants, which reveals that Dbp6p also functionally interacts with Rpl3p, Nop8p, and the so-far-uncharacterized Rsa3p (ribosome assembly 3). The nonessential Rsa3p is a predominantly nucleolar protein required for optimal biogenesis of 60S ribosomal subunits. Both Dbp6p and Rsa3p are associated with complexes that most likely correspond to early pre-60S ribosomal particles. Moreover, Rsa3p is co-immunoprecipitated with protA-tagged Dbp6p under low salt conditions. In addition, we have established a synthetic interaction network among factors involved in different aspects of 60S-ribosomal-subunit biogenesis. This extensive genetic analysis reveals that the rsa3 null mutant displays some specificity by being synthetically lethal with dbp6 alleles and by showing some synthetic enhancement with the nop8-101 and the rsa1 null allele.

scholarly journals Independent genes coding for three acidic proteins of the large ribosomal subunit from Saccharomyces cerevisiae.

1988 ◽  
Vol 263 (19) ◽  
pp. 9094-9101 ◽  
Author(s):  
M Remacha ◽  
M T Sáenz-Robles ◽  
M D Vilella ◽  
J P Ballesta
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Ribosomal Subunit ◽  
Large Ribosomal Subunit ◽  
Acidic Proteins

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.

Characterization of interaction sites in the Saccharomyces cerevisiae ribosomal stalk components

2002 ◽  
Vol 46 (3) ◽  
pp. 719-792 ◽  
Author(s):  
V. S. Lalioti ◽  
J. Pérez-Fernández ◽  
M. Remacha ◽  
J. P. G. Ballesta
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Interaction Sites ◽  
Ribosomal Stalk

scholarly journals Molecular genetics of cryptopleurine resistance in Saccharomyces cerevisiae: expression of a ribosomal protein gene family.

Genetics ◽  
1993 ◽  
Vol 135 (3) ◽  
pp. 719-730
Author(s):  
A G Paulovich ◽  
J R Thompson ◽  
J C Larkin ◽  
Z Li ◽  
J L Woolford
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Ribosomal Protein ◽  
Gene Fusion ◽  
Null Allele ◽  
Ribosomal Subunit ◽  
Null Alleles ◽  
Protein Synthesis Inhibitor ◽  
Lacz Gene ◽  
Ribosomal Subunits ◽  
Cry1 Gene

Abstract The Saccharomyces cerevisiae CRY1 gene encodes the 40S ribosomal subunit protein rp59 and confers sensitivity to the protein synthesis inhibitor cryptopleurine. A yeast strain containing the cry1-delta 1::URA3 null allele is viable, cryptopleurine sensitive (CryS), and expresses rp59 mRNA, suggesting that there is a second functional CRY gene. The CRY2 gene has been isolated from a yeast genomic library cloned in bacteriophage lambda, using a CRY1 DNA probe. The DNA sequence of the CRY2 gene contains an open reading frame encoding ribosomal protein 59 that differs at five residues from rp59 encoded by the CRY1 gene. The CRY2 gene was mapped to the left arm of chromosome X, centromere-proximal to cdc6 and immediately adjacent to ribosomal protein genes RPS24A and RPL46. Ribosomal protein 59 is an essential protein; upon sporulation of a diploid doubly heterozygous for cry1-delta 2::TRP1 cry2-delta 1::LEU2 null alleles, no spore clones containing both null alleles were recovered. Several results indicate that CRY2 is expressed, but at lower levels than CRY1: (1) Introduction of CRY2 on high copy plasmids into CryR yeast of genotype cry1 CRY2 confers a CryS phenotype. Transformation of these CryR yeast with CRY2 on a low copy CEN plasmid does not confer a CryS phenotype. (2) Haploids containing the cry1-delta 2::TRP1 null allele have a deficit of 40S ribosomal subunits, but cry2-delta 1::LEU2 strains have wild-type amounts of 40S ribosomal subunits. (3) CRY2 mRNA is present at lower levels than CRY1 mRNA. (4) Higher levels of beta-galactosidase are expressed from a CRY1-lacZ gene fusion than from a CRY2-lacZ gene fusion. Mutations that alter or eliminate the last amino acid of rp59 encoded by either CRY1 or CRY2 result in resistance to cryptopleurine. Because CRY2 (and cry2) is expressed at lower levels than CRY1 (and cry1), the CryR phenotype of cry2 mutants is only expressed in strains containing a cry1-delta null allele.

scholarly journals Pol5 is an essential ribosome biogenesis factor required for 60S ribosomal subunit maturation in Saccharomyces cerevisiae

RNA ◽  
2019 ◽  
Vol 25 (11) ◽  
pp. 1561-1575 ◽  
Author(s):  
Ana Ramos-Sáenz ◽  
Daniel González-Álvarez ◽  
Olga Rodríguez-Galán ◽  
Alfonso Rodríguez-Gil ◽  
Sonia G. Gaspar ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Ribosome Biogenesis ◽  
Ribosomal Subunit

Protein BmP0 from the silkworm Bombyx mori can be assembled and is functional in the Saccharomyces cerevisiae ribosomal stalk in the absence of the acidic P1 and P2 proteins

Gene ◽  
2003 ◽  
Vol 314 ◽  
pp. 173-179 ◽  
Author(s):  
Sophia Kouyanou ◽  
Cruz Santos ◽  
Vasiliki Koliaraki ◽  
Juan P.G Ballesta
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Bombyx Mori ◽  
Ribosomal Stalk ◽  
Silkworm Bombyx Mori

scholarly journals Fal1p is an essential DEAD-box protein involved in 40S-ribosomal-subunit biogenesis in Saccharomyces cerevisiae.

1997 ◽  
Vol 17 (12) ◽  
pp. 7283-7294 ◽  
Author(s):  
D Kressler ◽  
J de la Cruz ◽  
M Rojo ◽  
P Linder
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Translation Initiation ◽  
18S Rrna ◽  
Amino Acid Level ◽  
Ribosomal Subunit ◽  
Translation Initiation Factor ◽  
Initiation Factor ◽  
Northern Hybridization ◽  
Ribosomal Subunits ◽  
Dead Box

A previously uncharacterized Saccharomyces cerevisiae gene, FAL1, was found by sequence comparison as a homolog of the eukaryotic translation initiation factor 4A (eIF4A). Fal1p has 55% identity and 73% similarity on the amino acid level to yeast eIF4A, the prototype of ATP-dependent RNA helicases of the DEAD-box protein family. Although clearly grouped in the eIF4A subfamily, the essential Fal1p displays a different subcellular function and localization. An HA epitope-tagged Fal1p is localized predominantly in the nucleolus. Polysome analyses in a temperature-sensitive fal1-1 mutant and a Fal1p-depleted strain reveal a decrease in the number of 40S ribosomal subunits. Furthermore, these strains are hypersensitive to the aminoglycoside antibiotics paromomycin and neomycin. Pulse-chase labeling of pre-rRNA and steady-state-level analysis of pre-rRNAs and mature rRNAs by Northern hybridization and primer extension in the Fal1p-depleted strain show that Fal1p is required for pre-rRNA processing at sites A0, A1, and A2. Consequently, depletion of Fal1p leads to decreased 18S rRNA levels and to an overall deficit in 40S ribosomal subunits. Together, these results implicate Fal1p in the 18S rRNA maturation pathway rather than in translation initiation.

scholarly journals Different roles of P1 and P2 Saccharomyces cerevisiae ribosomal stalk proteins revealed by cross-linking

2006 ◽  
Vol 62 (4) ◽  
pp. 1191-1202 ◽  
Author(s):  
Deyi Qiu ◽  
Pilar Parada ◽  
Alberto García Marcos ◽  
David Cárdenas ◽  
Miguel Remacha ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cross Linking ◽  
Ribosomal Stalk
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