Dear Editor,The passage of DNA replication forks during eukaryotic cell division disrupts the nucleosomes they encounter,and de novo assembly of nucleosomes onto replicated DNA must take place to restore chromatin str...Dear Editor,The passage of DNA replication forks during eukaryotic cell division disrupts the nucleosomes they encounter,and de novo assembly of nucleosomes onto replicated DNA must take place to restore chromatin structure.There are two sources of histones for the replicationcoupled nucleosome assembly.展开更多
TRIM71 is an RNA-binding protein with ubiquitin ligase activity.Numerous functions of mammalian TRIM71,including cell cycle regulation,embryonic stem cell(ESC)self-renewal,and reprogramming of pluripotent stem cells,a...TRIM71 is an RNA-binding protein with ubiquitin ligase activity.Numerous functions of mammalian TRIM71,including cell cycle regulation,embryonic stem cell(ESC)self-renewal,and reprogramming of pluripotent stem cells,are related to its RNA-binding property.We previously reported that a long noncoding RNA(lnc RNA)Trincr1 interacts with mouse TRIM71(m TRIM71)to repress FGF/ERK pathway in mouse ESCs(m ESCs).Herein,we identify an RNA motif specifically recognized by m TRIM71 from Trincr1 RNA,and solve the crystal structure of the NHL domain of m TRIM71 complexed with the RNA motif.Similar to the zebrafish TRIM71,m TRIM71 binds to a stem-loop structured RNA fragment of Trincr1,and an adenosine base at the loop region is crucial for the m TRIM71 interaction.We map similar hairpin RNAs preferably bound by TRIM71 in the m RNA UTRs of the cell-cycle related genes regulated by TRIM71.Furthermore,we identify key residues of m TRIM71,conserved among mammalian TRIM71 proteins,required for the RNA-binding property.Single-site mutations of these residues significantly impair the binding of TRIM71 to hairpin RNAs in vitro and to m RNAs of Cdkn1a/p21 and Rbl2/p130 in m ESCs.Furthermore,congenital hydrocephalus(CH)specific mutation of m TRIM71 impair its binding to the RNA targets as well.These results reveal molecular mechanism behind the recognition of RNA by mammalian TRIM71 and provide insights into TRIM71 related diseases.展开更多
Sequence-specific transcription factors(TFs)selectively bind to the regulatory regions of target genes to regulate gene expression.Although an old topic,how TFs specifically and efficiently identify and bind to their ...Sequence-specific transcription factors(TFs)selectively bind to the regulatory regions of target genes to regulate gene expression.Although an old topic,how TFs specifically and efficiently identify and bind to their target sequences is not fully understood.The dominant idea holds that TFs bind short sequence-specific DNA motifs within regulatory regions via direct base interactions andDNA shape recognition[1].展开更多
Faithful DNA duplication is the fundamental event for all life forms.How to replicate the whole genome quickly and efficiently is a challenge that must be faced within every S phase of the cell cycle[1].Considering th...Faithful DNA duplication is the fundamental event for all life forms.How to replicate the whole genome quickly and efficiently is a challenge that must be faced within every S phase of the cell cycle[1].Considering the increased size and complexity of mammalian genomes,it is plausible that the regulation of DNA replication is more intricate in mammals.Tens of thousands of replication origins have been identified throughout mammalian genomes[2].Whether replication forks originated from different origins cooperate during replication is a long-term concern in the field.展开更多
Eukaryotic cell division duplicates the chromosomes in the parental cell and equally segregates sister chromatids into daughter cells.This process involves the replication of chromosomal DNA and packaging the replicat...Eukaryotic cell division duplicates the chromosomes in the parental cell and equally segregates sister chromatids into daughter cells.This process involves the replication of chromosomal DNA and packaging the replicated DNA in nucleosomes,which consist of~147 base pairs(bp)of DNA wrapped around an octamer of histones H2A,H2B,H3,and H4[1].展开更多
The Integrator complex,discovered in 2005 while searching for protein partners of deleted in split hand/split foot protein 1(DSS1),is the exclusive large multiprotein complex associated with RNA PolⅡthat is specific ...The Integrator complex,discovered in 2005 while searching for protein partners of deleted in split hand/split foot protein 1(DSS1),is the exclusive large multiprotein complex associated with RNA PolⅡthat is specific to metazoans[1].展开更多
基金supported by the National Key Research and Development Program of China(2019YFA0508900)the National Natural Science Foundation of China(32330021,31991162,32200477)the Strategic Priority Research Program of Chinese Academy of Sciences(XDB37010100)。
文摘Dear Editor,The passage of DNA replication forks during eukaryotic cell division disrupts the nucleosomes they encounter,and de novo assembly of nucleosomes onto replicated DNA must take place to restore chromatin structure.There are two sources of histones for the replicationcoupled nucleosome assembly.
基金the Chinese Ministry of Science and Technology,the National Natural Science Foundation of China(2019YFA0508902,32170549,32371315,2021YFA1100200,and 91940302)Haihe Laboratory of Cell Ecosystem Innovation Fund(22HHXBSS00021)。
文摘TRIM71 is an RNA-binding protein with ubiquitin ligase activity.Numerous functions of mammalian TRIM71,including cell cycle regulation,embryonic stem cell(ESC)self-renewal,and reprogramming of pluripotent stem cells,are related to its RNA-binding property.We previously reported that a long noncoding RNA(lnc RNA)Trincr1 interacts with mouse TRIM71(m TRIM71)to repress FGF/ERK pathway in mouse ESCs(m ESCs).Herein,we identify an RNA motif specifically recognized by m TRIM71 from Trincr1 RNA,and solve the crystal structure of the NHL domain of m TRIM71 complexed with the RNA motif.Similar to the zebrafish TRIM71,m TRIM71 binds to a stem-loop structured RNA fragment of Trincr1,and an adenosine base at the loop region is crucial for the m TRIM71 interaction.We map similar hairpin RNAs preferably bound by TRIM71 in the m RNA UTRs of the cell-cycle related genes regulated by TRIM71.Furthermore,we identify key residues of m TRIM71,conserved among mammalian TRIM71 proteins,required for the RNA-binding property.Single-site mutations of these residues significantly impair the binding of TRIM71 to hairpin RNAs in vitro and to m RNAs of Cdkn1a/p21 and Rbl2/p130 in m ESCs.Furthermore,congenital hydrocephalus(CH)specific mutation of m TRIM71 impair its binding to the RNA targets as well.These results reveal molecular mechanism behind the recognition of RNA by mammalian TRIM71 and provide insights into TRIM71 related diseases.
基金the National Natural Science Foundation of China(32288102)the New Cornerstone Science Laboratory。
文摘Sequence-specific transcription factors(TFs)selectively bind to the regulatory regions of target genes to regulate gene expression.Although an old topic,how TFs specifically and efficiently identify and bind to their target sequences is not fully understood.The dominant idea holds that TFs bind short sequence-specific DNA motifs within regulatory regions via direct base interactions andDNA shape recognition[1].
文摘Faithful DNA duplication is the fundamental event for all life forms.How to replicate the whole genome quickly and efficiently is a challenge that must be faced within every S phase of the cell cycle[1].Considering the increased size and complexity of mammalian genomes,it is plausible that the regulation of DNA replication is more intricate in mammals.Tens of thousands of replication origins have been identified throughout mammalian genomes[2].Whether replication forks originated from different origins cooperate during replication is a long-term concern in the field.
基金supported by National Key R&D Program of China(2021YFF0704500,2021YFF0703701,and 2022YFC3400405)the Strategic Priority Research Program of the Chinese Academy of Sciences(XDB38040300)+4 种基金the 14th Five-year Informatization Plan of Chinese Academy of Sciences(CASWX2021SF-0203)the National Natural Science Foundation of China(91940306,31871294,31970647,81902519,and 32200478)the Special Investigation on Science and Technology Basic Resources of the MOST,China(2019FY100102)the China Postdoctoral Science Foundation(2022M713311)the National Genomics Data Center,China。
基金supported by the Ministry of Science and Technology of China(2019YFA0508900)the National Natural Science Foundation of China(32170549 and 32371315)+1 种基金Haihe Laboratory of Cell Ecosystem Innovation Fund(22HHXBSS00021)Chinese Academy of Sciences Youth Innovation Promotion Association grants(2017131)。
文摘Eukaryotic cell division duplicates the chromosomes in the parental cell and equally segregates sister chromatids into daughter cells.This process involves the replication of chromosomal DNA and packaging the replicated DNA in nucleosomes,which consist of~147 base pairs(bp)of DNA wrapped around an octamer of histones H2A,H2B,H3,and H4[1].
基金supported by the National Natural Science Foundation of China(32288102)the New Cornerstone Science Laboratory。
文摘The Integrator complex,discovered in 2005 while searching for protein partners of deleted in split hand/split foot protein 1(DSS1),is the exclusive large multiprotein complex associated with RNA PolⅡthat is specific to metazoans[1].
