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Search results 101 to 127 out of 127 for Bms1

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0.019s
Type Details Score
Gene
Type: gene
Organism: macaque, rhesus
Gene
Type: gene
Organism: macaque, rhesus
Gene
Type: gene
Organism: macaque, rhesus
Gene
Type: gene
Organism: macaque, rhesus
Gene
Type: gene
Organism: dog, domestic
Gene
Type: gene
Organism: chimpanzee
Gene
Type: gene
Organism: chimpanzee
Gene
Type: gene
Organism: chimpanzee
Gene
Type: gene
Organism: chimpanzee
Gene
Type: gene
Organism: chimpanzee
Gene
Type: gene
Organism: chimpanzee
DO Term
Publication
First Author: Karbstein K
Year: 2006
Journal: J Mol Biol
Title: GTP-dependent formation of a ribonucleoprotein subcomplex required for ribosome biogenesis.
Volume: 356
Issue: 2
Pages: 432-43
Protein Domain
Type: Domain
Description: Bms1 is an essential, evolutionarily conserved, nucleolar protein. Its depletion interferes with processing of the 35S pre-rRNA at sites A0, A1, and A2, and the formation of 40S subunits. Bms1, the putative endonuclease Rc11, and the essential U3 small nucleolar RNA form a stable subcomplex that is believed to control an early step in the formation of the 40S subunit []. The N terminus of Bms1 contains a guanine nucleotide-binding (G) domain that functions intramolecularly. It is believed that Rc11 activates Bms1 by acting as a guanine-nucleotide exchange factor (GEF) to promote GDP/GTP exchange, and that activated (GTP-bound) Bms1 delivers Rc11 to the preribosomes [].This entry represents the N-terminal domain of Bms1.
Protein Domain
Type: Domain
Description: This domain is found at the C terminus of the ribosome biogenesis protein BMS1 and TSR1 families, which may act as a molecular switch during maturation of the 40S ribosomal subunit in the nucleolus.
Publication
First Author: Wegierski T
Year: 2001
Journal: RNA
Title: Bms1p, a G-domain-containing protein, associates with Rcl1p and is required for 18S rRNA biogenesis in yeast.
Volume: 7
Issue: 9
Pages: 1254-67
Protein
Organism: Mus musculus/domesticus
Length: 803  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1284  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1287  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 1223  
Fragment?: true
Protein Domain
Type: Domain
Description: Bms1p and Tsr1p represent a new family of factors required for ribosomebiogenesis. They are each independently required for 40S ribosomal subunitbiogenesis. Bms1p, a protein required for pre-rRNA processing, contains anevolutionarily conserved guanine nucleotide-binding (G) domain with five conserved polypeptide loopsdesignated G1 through G5, which form contact sites with the guanine nucleotideor coordinate the Mg(2+) ion. Sequences resembling G1 (consensus [GA]-x(4)-G-K-[ST]; also known as a P-loop), G4 (consensus [NT]-K-x-D), and G5 (consensusS-[AG]are present in all Bms1 proteins, and either fully conform with theconsensus or contain, at most, single conservative substitutions. The G2 motif(consensus G-P-[IV]-T) contains a T residue involved in the coordination ofthe Mg(2+) required for GTP hydrolysis. The G3 motif diverges from theconsensus found in G proteins, D-x(2)-G; however, the D residue is replacedwith the conserved E residue. In contrast, Tsr1p lacks a P-loop and is notpredicted to bind GTP. It functions at a later step of 40S ribosomeproduction, possibly in assembly and/or export of 43S pre-ribosomal subunitsto the cytosol [, , ].This entry represents a domain found in Bms1 and Tsr1, and includes cases, such as Tsr1, where it may not function as a guanine nucleotide-binding domain.
Protein
Organism: Mus musculus/domesticus
Length: 830  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 416  
Fragment?: true
Publication
First Author: Gelperin D
Year: 2001
Journal: RNA
Title: Bms1p, a novel GTP-binding protein, and the related Tsr1p are required for distinct steps of 40S ribosome biogenesis in yeast.
Volume: 7
Issue: 9
Pages: 1268-83
Protein Domain
Type: Family
Description: Bms1p and Tsr1p represent a new family of factors required for ribosomebiogenesis. They are each independently required for 40S ribosomal subunitbiogenesis. Bms1p, a protein required for pre-rRNA processing, contains anevolutionarily conserved guanine nucleotide-binding (G) domain with five conserved polypeptide loopsdesignated G1 through G5, which form contact sites with the guanine nucleotideor coordinate the Mg(2+) ion. Sequences resembling G1 (consensus [GA]-x(4)-G-K-[ST]; also known as a P-loop), G4 (consensus [NT]-K-x-D), and G5 (consensusS-[AG]are present in all Bms1 proteins, and either fully conform with theconsensus or contain, at most, single conservative substitutions. The G2 motif(consensus G-P-[IV]-T) contains a T residue involved in the coordination ofthe Mg(2+) required for GTP hydrolysis. The G3 motif diverges from theconsensus found in G proteins, D-x(2)-G; however, the D residue is replacedwith the conserved E residue. In contrast, Tsr1p lacks a P-loop and is notpredicted to bind GTP. It functions at a later step of 40S ribosomeproduction, possibly in assembly and/or export of 43S pre-ribosomal subunitsto the cytosol [, , ].
Publication
First Author: Leipe DD
Year: 2002
Journal: J Mol Biol
Title: Classification and evolution of P-loop GTPases and related ATPases.
Volume: 317
Issue: 1
Pages: 41-72
Publication
First Author: Gerhard DS
Year: 2004
Journal: Genome Res
Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Volume: 14
Issue: 10B
Pages: 2121-7