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Literature summary extracted from

  • De, I.; Bessonov, S.; Hofele, R.; dos Santos, K.; Will, C.L.; Urlaub, H.; Luehrmann, R.; Pena, V.
    The RNA helicase Aquarius exhibits structural adaptations mediating its recruitment to spliceosomes (2015), Nat. Struct. Mol. Biol., 22, 138-144 .
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.6.4.13 RNA Aquarius hydrolyzes ATP, and this activity is highly stimulated in the presence of a 22-nt RNA with a random sequence. Aquarius does not bind a blunt-ended RNA duplex, and correspondingly the latter does not stimulate Aquarius's ATPase activity Homo sapiens

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.6.4.13 purified recombinant enzyme Aquanrius, X-ray diffraction structure determination and analysis at 2.3 A resolution Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
3.6.4.13 K829A site-directed mutagenesis, mutation of the invariant lysine residue from motif I involved in ATP binding and hydrolysis drastically reduced Aquarius's ability to bind ATP and ADP and to hydroxadlyze ATP, the mutant shows significantly reduced ATPase activity compared to wild-type enzyme Homo sapiens
3.6.4.13 Y1196A site-directed mutagenesis, mutation of a conserved aromatic residue located near the putative RNA-binding surface of the RecA2 inhibits Aquarius's RNA-unwinding activity without changing its RNA-binding and ATPase properties, a helicase-deficient mutant Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.6.4.13 AMP-PNP structure of Aquarius in complex with AMP-PNP, modelling, overview Homo sapiens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.6.4.13 nucleus
-
Homo sapiens 5634
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.6.4.13 Mg2+ required Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.6.4.13 ATP + H2O Homo sapiens
-
ADP + phosphate
-
?
3.6.4.13 additional information Homo sapiens multiple cross-links between Aquarius and hSyf1, hIsy1, CCDC16 or CypE, with the majority of the cross-linked residues located in domains or structural insertions specific for Aquarius, such as the ARM, pointer and thumb domains, and in the large insertions of the beta-barrel ?
-
-

Organism

EC Number Organism UniProt Comment Textmining
3.6.4.13 Homo sapiens O60306
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.6.4.13 HeLa cell
-
Homo sapiens
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.6.4.13 ATP + H2O
-
Homo sapiens ADP + phosphate
-
?
3.6.4.13 additional information multiple cross-links between Aquarius and hSyf1, hIsy1, CCDC16 or CypE, with the majority of the cross-linked residues located in domains or structural insertions specific for Aquarius, such as the ARM, pointer and thumb domains, and in the large insertions of the beta-barrel Homo sapiens ?
-
-
3.6.4.13 additional information Aquarius exhibits ATPase and RNA-unwinding activity in vitro. Consistently with its possessing a Q motif and thus specifically binding ATP, Aquarius does not hydrolyze GT. Aquarius does not bind a blunt-ended RNA duplex Homo sapiens ?
-
-

Subunits

EC Number Subunits Comment Organism
3.6.4.13 More enzyme Aquarius is integrated into the spliceosome as part of the intron-binding complex (IBC). The ARM domain is essential for IBC formation Homo sapiens
3.6.4.13 pentamer
-
Homo sapiens

Synonyms

EC Number Synonyms Comment Organism
3.6.4.13 Aquarius
-
Homo sapiens
3.6.4.13 DExH/D-box RNA helicase
-
Homo sapiens
3.6.4.13 IBP160
-
Homo sapiens
3.6.4.13 intron-binding protein 160
-
Homo sapiens
3.6.4.13 RNA helicase Aquarius
-
Homo sapiens

General Information

EC Number General Information Comment Organism
3.6.4.13 malfunction an ATPase-deficient Aquarius mutant hinders splicing Homo sapiens
3.6.4.13 metabolism the spliceosome's structural rearrangements are driven by eight conserved DExH/D-box RNA helicases that contain two RecA-like domains, which form a motor module required for ATP hydrolysis, RNA unwinding and coupling of these two processes. RNA helixadcases can have very diverse functions, including proofreading specific steps of pre-mRNA splicing. Most helicases also conxadtain specific accessory domains important for their regulation or task-specific function. The human spliceosome contains five addixadtional RNA helicases (Aquarius, SF3b125, elFAIII and DDX35 and Abstrakt). Multiple cross-links between Aquarius and hSyf1, hIsy1, CCDC16 or CypE, with the majority of the cross-linked residues located in domains or structural insertions specific for Aquarius, such as the ARM, pointer and thumb domains, and in the large insertions of the beta-barrel. The for intron-binding complex (IBC) is cross-linked to U2 SF3a and SF3b proteins, interaction partners of the IBC in the spliceosome. The Aquarius ARM domain is cross-linked to SF3b155 Homo sapiens
3.6.4.13 additional information the SF1 core of Aquarius consists of two RecA-like domains, an alpha-helical stalk and a beta-barrel domain. The canonical sequence motifs of RNA helicases are conserved, and the ATP analogue binds with the adenine sandwiched between Leu1157 and Ile800. The amino group of the adenine is recognized by Gln806 from the Q motif, a distinctive feature of helicases able to use only ATP. The space between the RecA1, RecA2, beta-barrel and a domain that we denote as an armadillo (ARM) domain is filled by the so-called stalk, a structural unit encompassing 125 residues (416-492 and 660-710) exhibiting helixadces, extensive coils and loops. The large surfaces that the stalk shares with other domains suggest that it has a key architectural role. Notably, numerous large hydrophobic residues that mediate these contacts are highly conxadserved. Aquarius's ARM domain is required for intron-binding complex (IBC) formation Homo sapiens
3.6.4.13 physiological function RNA helicase Aquarius is crucial for the assembly of box C and box D (box C/D) small nucleolar RNPs (snoRNPs), whose small nucleolar RNAs (snoRNAs) are found in introns about 50 nt upstream of the BS, i.e., 10 nt upstream of Aquarius's binding site. The ATP hydrolysis by Aquarius is required for efficient pre-mRNA splicing Homo sapiens