Identifiers and Description

Gene Model Identifier

Contig6660.g7128

Standard Name

DEAD3 (REQL, DEAD/DEAH box helicase)

Aliases

None

Description

REQL, DEAD/DEAH box helicase

Genome Browser

GBrowse

Gene Ontology Annotations

Molecular Function

Biological Process

  • mesodermal cell migration (IEA) | GO:0008078
  • obsolete mitochondrial aspartate/glutamate transport (IEA) | GO:0006845
  • negative regulation of gibberellic acid mediated signaling pathway (IEA) | GO:0009938

Domains

No Data fetched for Domains

Gene Expression Profile

No expression data available at this time.

Homologs

No Data fetched for Homologs

General Information

Paragraph NoGene NameParagraph Text
13DEAD31. Gene. 2012 Apr 15;497(2):147-54. doi: 10.1016/j.gene.2012.01.068. Epub 2012 Feb 2. A telomerase-associated RecQ protein-like helicase resolves telomeric G-quadruplex structures during replication. Postberg J(1), Tsytlonok M, Sparvoli D, Rhodes D, Lipps HJ. Author information: (1)Centre for Biomedical Education and Research, Institute of Cell Biology, Witten, Germany. It is well established that G-quadruplex DNA structures form at ciliate telomeres and their formation throughout the cell-cycle by telomere-end-binding proteins (TEBPs) has been analyzed. During replication telomeric G-quadruplex structure has to be resolved to allow telomere replication by telomerase. It was shown that both phosphorylation of TEBPβ and binding of telomerase are prerequisites for this process, but probably not sufficient to unfold G-quadruplex structure in timely manner to allow replication to proceed. Here we describe a RecQ-like helicase required for unfolding of G-quadruplex structures in vivo. This helicase is highly reminiscent of human RecQ protein-like 4 helicase as well as other RecQ-like helicase found in various eukaryotes and E. coli. In situ analyses combined with specific silencing of either the telomerase or the helicase by RNAi and co-immunoprecipitation experiments demonstrate that this helicase is associated with telomerase during replication and becomes recruited to telomeres by this enzyme. In vitro assays showed that a nuclear extract prepared from cells in S-phase containing both the telomerase as well as the helicase resolves telomeric G-quadruplex structure. This finding can be incorporated into a mechanistic model about the replication of telomeric G-quadruplex structures during the cell cycle. Copyright © 2012 Elsevier B.V. All rights reserved. PMCID: PMC3650557 PMID: 22327026 [PubMed - indexed for MEDLINE]

Associated Literature

No Data fetched for Associated Literature

Sequences

>Contig6660.g7128(protein)
MNSIIKKFQDRGIKSGHYVNPSKQNETIAQKNQTQASDAFSKQKSMTNAGSGVLTKQQIP
NTAGLKAHQNPIMQKQQVGIPNISRKAVTSVDSRQPSKKQNQSMIPASKAVGKKKFNLDA
MMYNPTDDLKIDNAATIFIEREKQHKVEKSYEEPSTAINEPEQNIENSIMQTFSRLNQRI
ASAQAKMAKNLPNKSKENANNNSENVSTFNDQTLKVPGYQSFHNADQLINTADHSDIKNT
QKTLFNSNFGNSDSTNLMSSAQQSAQTRPSISNQMTTPSDNYQTSQFTLNILGESGKASA
KNNQETPKQFNQNPSKLTKIQETDEEGNRMSILPSKKRPSIVPSTGKKAPSVKKAKVKST
KQTDKQANIEGNEEKKSNTIMDKMKTQVDKLKESKPISKNPSNTQQRTNFVKMNMNNYKP
RMRGGAFQNKMMAKKKNYLKFNERMKKKLMIENAKHRDQVNAYGGLGKVGLDHQGGTKEM
VDAEGNAIEDLVPGFSTSALKYVRKLKQLSEIDINEDDENLLIDDLEQMKADLEKIDEDI
KEDIVEVSSDFDKPLYKIPSSDEEYQKILKERFGHETFKAGQLEAIKILLEKKQNALVVL
ATGGGKSLVYQYVSMFLQGLVLIVTPLISLMTDQLGKLPDFLPGASLNSQQNYQLKKEVI
KAIQDKHIKILFISPEKFFIEDFSKYNRKIAMVCVDEIHCASEWSHNFRPAYLKLHDMIK
EKVSNQQDNCVVMGLTATATKATQRSVCKIFDVKYPDHIVTEANLSRMNLSLSITRDQDK
LKSLLALLASNSFKKLTSILIFATHKGTCERLASHLNIRVLVCTIAFSMGIDKSDIQSVI
HYDMPKSIENYVQEIGRAGRDGKLARCHLFLCNEDFYLIRRLILTDILDNQNALKLTNKI
VVEFKKTLLKIINPTLAKSKKRKLKSISGAEEKHDQLIEEFEHEEEIKNYYEGSENDAKK
IYPSSIKQIENPDRVYLFLDIKDTLEMLDLKKEVVLTMLNSLEKLTDEKKFFRLEGILPE
KIGLRFHNKRPEQMAKDNSFIRKFMEIAKEHQGVYNVSTQRLAYELNMNPFQIPKILFSL
QNTEHGDISYDTDQDSFVLRLQHIPSGGSTFDLSQDMLTETRRIERNMIQKLNCMYFVAR
KVSLPSVEYMLKKEKQEDSMDMYKAYSQQLNDLINLYFGIEQEENMEIQIAGSEQERNLM
MPLLYIDSHRDKANVEVITYSRIQQFQSEIKQVLKEFYDQNPGQIDGNDRLKPLDIVKIL
MGIYSDRSNVKRFANNSRVWAKLQEYDYEDVFKVAIATVNQYYLDVLSGNGSSKIDMMPK
DIIEGEASKKRKLN


>Contig6660.g7128(coding)
atgaactcaattatcaaaaagttttaagacagaggcataaaatctggacattatgtcaac
ccttctaaacaaaatgaaactatagcgtaaaaaaatcaaactcaagcttctgatgcattt
agtaaacagaaatcaatgactaatgctggttcaggggttctcaccaagcaataaattcca
aatacagctggtctaaaagctcattaaaatcccataatgtagaagtaataagtaggtatt
ccgaacatatcgagaaaagcagtaacatcagtcgattccagacaaccttctaaaaaataa
aatcagtcaatgataccagcatccaaagctgtagggaagaaaaagttcaaccttgatgct
atgatgtacaatcccactgatgatttgaaaatagataatgccgcgacgatttttattgag
cgggaaaagtaacataaagttgaaaagtcatatgaggagccttcaactgcaattaatgaa
ccagagtaaaatattgaaaattccatcatgcaaacattcagcagactcaatcaaaggatc
gcctcagcttaagccaaaatggcaaagaaccttccaaataaaagtaaagaaaacgcaaat
aataactctgaaaatgtgagcactttcaatgattaaactttgaaagttccagggtatcaa
agttttcacaatgcagattagcttatcaatactgctgatcactcagacattaagaatact
tagaaaaccctctttaattctaattttggcaactctgatagcaccaatctgatgagtagc
gcttagtaaagtgcttagactagacctagcatcagcaattaaatgactaccccctctgat
aattatcaaacctcccaatttactctcaatattttaggggaaagtgggaaagcttctgct
aagaataactaagaaactcctaaacagtttaattaaaacccctcaaaattgacgaaaatt
caggaaactgatgaagaaggcaacagaatgagtatccttccttcaaagaagcgacctagc
atcgttccaagcactggtaagaaagctccaagtgtcaagaaagcaaaagtaaagtcaacg
aaacaaactgataaacaagcaaatattgagggaaatgaagagaagaaaagcaataccata
atggataagatgaaaactcaagtagacaagttgaaggaatcaaaacctatctctaagaac
ccttcaaacacccagcagagaactaacttcgtgaagatgaatatgaataattataaacct
agaatgagaggtggagcattctaaaataagatgatggctaagaagaaaaattacttgaag
tttaatgaaagaatgaagaaaaagctaatgattgaaaatgctaaacatcgtgactaagta
aatgcctatggtggattaggaaaggtaggacttgatcatcagggtggaactaaagaaatg
gttgatgctgagggaaatgcaattgaggatttggtgccaggattcagcacttctgctttg
aaatatgtgagaaaacttaagtaattaagtgaaatcgatataaatgaagatgatgaaaat
ttgctgattgatgacttggaataaatgaaagctgatctcgaaaagatcgatgaagatatc
aaagaggatatagtagaagtttcctcagacttcgataaaccactctataaaattccatca
tctgatgaagagtaccagaaaatattgaaagaaagatttggacatgaaactttcaaggca
ggtcagcttgaagcgatcaaaatcttattggagaaaaagcaaaatgctttggttgtatta
gctactggaggaggtaaatcattagtctatcaatacgtatcaatgttcctgcaaggactt
gtacttatagttactcctctaatttctttgatgactgatcaacttggaaaattgccagat
ttcttgccaggagcatcattgaactcttagtaaaattaccaactcaaaaaagaagtaatt
aaagcaatttaggacaagcacatcaagattttattcatttctccagagaagtttttcatt
gaagatttcagcaagtacaatcgtaaaattgcaatggtttgtgtagatgagatccattgt
gcttcagaatggtctcataatttcagaccagcttacctaaagttgcatgatatgattaag
gaaaaggtgagcaatcagcaagacaattgtgttgtaatgggacttacagcaacagcaacc
aaagcaacctagagatcggtatgcaagattttcgatgttaagtatccagatcatatcgta
actgaggctaatctgtcaagaatgaatctaagtctcagtatcacaagagattaagataag
ttaaagtcacttttagctttacttgcttctaatagtttcaagaaacttacatctatacta
atatttgccactcacaagggtacttgtgaaagactagctagtcatctcaatatccgagtg
ctcgtttgcacaattgccttctctatgggtatagataagtctgacattcaatcagtcatt
cattacgatatgcctaagtctattgagaactatgtttaagagattggacgtgctggcaga
gatggtaaacttgcaagatgccatttattcctttgcaatgaagatttctacttgataaga
agactaattctcacagatattcttgacaaccaaaatgcattgaaattaaccaacaagata
gtagttgagtttaagaaaacacttttaaagattataaacccgacattagctaagtccaaa
aagagaaagcttaagtcaattagtggcgctgaggaaaagcatgactaattaattgaagaa
tttgaacatgaagaagaaatcaagaattattatgaaggctctgaaaatgatgcaaagaag
atatatccaagttctataaaataaattgagaatcctgatagagtttatttattcttagac
attaaggataccctagaaatgctagacttaaagaaagaggtagtgttgacaatgctaaat
tctcttgaaaagctaacagacgaaaagaaattctttagactagagggaatcttacctgaa
aagataggccttagattccataataaaagacctgaataaatggcaaaagataattctttc
atcagaaagtttatggaaatagctaaggagcattaaggagtctacaatgtaagcacttag
agattagcatatgagctgaatatgaatccattccaaataccaaaaatcctcttctcatta
caaaatactgaacatggagatatatcctacgatacagactaagatagctttgttctaaga
cttcaacatattccaagtggtggatctacttttgatctatcttaggatatgctaactgag
acgagaagaattgaaagaaacatgatttaaaaactgaattgcatgtatttcgttgcaaga
aaagtgagtctaccttctgtagagtatatgcttaaaaaagagaagcaagaagattccatg
gatatgtacaaagcttattcacaataactgaatgatctcatcaacttgtacttcggcatt
gagtaggaagaaaacatggaaatatagattgctggaagtgagcaagagaggaatctaatg
atgcctttattatacatagattcacatcgcgataaagctaatgttgaggtaattacatat
tcaagaatataacaattttagagcgaaataaagcaagtattgaaagaattctatgactaa
aacccaggctaaatagatggcaatgacagactaaaaccacttgatattgtcaagatatta
atgggtatatatagcgatagatcaaatgtaaagaggttcgctaacaatagcagagtctgg
gccaaattataagaatacgactatgaggatgttttcaaggttgctatagcaactgttaac
taatattatctcgatgtgcttagcggtaacggtagtagtaaaatagatatgatgcccaag
gacatcatagaaggtgaggcttctaagaagagaaaattaaactga