Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2010-2-1
pubmed:abstractText
Maternal effect genes and encoding proteins are necessary for nuclear reprogramming and zygotic genome activation. However, the mechanisms that mediate these functions are largely unknown. Here we identified XM_359149, a Zar1-like gene that is predominantly expressed in oocytes and zygotes, which we designated Zar1-like (Zar1l). ZAR1L-EGFP formed multiple cytoplasmic foci in late two-cell-stage embryos. Expression of the ZAR1L C-terminus induced two-cell-stage embryonic arrest, accompanied with abnormal methylation of histone H3K4me2/3 and H3K9me2/3, and marked down-regulation of a group of chromatin modification factors including Dppa2, Dppa4, and Piwil2. When ectopically expressed in somatic cells, ZAR1L colocalized with P-body components including EIF2C1(AGO1), EIF2C2(AGO2), DDX6 and LSM14A, and germline-specific chromatoid body components including PIWIL1, PIWIL2, and LIN28. ZAR1L colocalized with ZAR1 and interacted with human LIN28. Our data suggest that ZAR1L and ZAR1 may comprise a novel family of processing-body/chromatoid-body components that potentially function as RNA regulators in early embryos.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Argonaute Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Bromodeoxyuridine, http://linkedlifedata.com/resource/pubmed/chemical/DEAD-box RNA Helicases, http://linkedlifedata.com/resource/pubmed/chemical/Ddx6 protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/EIF2C2 protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/Egg Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Eukaryotic Initiation Factor-2, http://linkedlifedata.com/resource/pubmed/chemical/Eukaryotic Initiation Factors, http://linkedlifedata.com/resource/pubmed/chemical/Histones, http://linkedlifedata.com/resource/pubmed/chemical/LIN-28 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Lin-28 protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/Piwil1 protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/Piwil2 protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins, http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger, http://linkedlifedata.com/resource/pubmed/chemical/RNA Polymerase II, http://linkedlifedata.com/resource/pubmed/chemical/RNA-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Zar1 protein, mouse
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
1097-0177
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
239
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
407-24
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed-meshheading:20014101-Amino Acid Sequence, pubmed-meshheading:20014101-Animals, pubmed-meshheading:20014101-Argonaute Proteins, pubmed-meshheading:20014101-Bromodeoxyuridine, pubmed-meshheading:20014101-Cell Line, pubmed-meshheading:20014101-DEAD-box RNA Helicases, pubmed-meshheading:20014101-Egg Proteins, pubmed-meshheading:20014101-Embryo, Mammalian, pubmed-meshheading:20014101-Embryonic Development, pubmed-meshheading:20014101-Eukaryotic Initiation Factor-2, pubmed-meshheading:20014101-Eukaryotic Initiation Factors, pubmed-meshheading:20014101-Female, pubmed-meshheading:20014101-Gene Expression Regulation, Developmental, pubmed-meshheading:20014101-Histones, pubmed-meshheading:20014101-Humans, pubmed-meshheading:20014101-Male, pubmed-meshheading:20014101-Mice, pubmed-meshheading:20014101-Mice, Inbred C57BL, pubmed-meshheading:20014101-Mice, Inbred DBA, pubmed-meshheading:20014101-Molecular Sequence Data, pubmed-meshheading:20014101-Mutation, pubmed-meshheading:20014101-Proteins, pubmed-meshheading:20014101-Proto-Oncogene Proteins, pubmed-meshheading:20014101-RNA, Messenger, pubmed-meshheading:20014101-RNA Polymerase II, pubmed-meshheading:20014101-RNA-Binding Proteins, pubmed-meshheading:20014101-Sequence Alignment
pubmed:year
2010
pubmed:articleTitle
Mouse ZAR1-like (XM_359149) colocalizes with mRNA processing components and its dominant-negative mutant caused two-cell-stage embryonic arrest.
pubmed:affiliation
The Department of Cell Biology and Genetics, College of Life Sciences, Peking University, Beijing, People's Republic of China.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't