Slime formation on paper machines is a critical issue that can substantially impact the quantity and quality of paper production.This problem is caused by the growth of an abundant and diverse amount of bacteria.Throu...Slime formation on paper machines is a critical issue that can substantially impact the quantity and quality of paper production.This problem is caused by the growth of an abundant and diverse amount of bacteria.Through the application of emulsion polymerase chain reaction(emPCR),the bacterial diversity was analyzed on paper machines and more operational taxonomic units(OTUs)were obtained.Eleven types of bacterial phyla were found that have been previously identified,including Proteobacteria(α-,β-,γ-,ε-,andφ-),Bacteroidetes,Firmicutes,Cyanobacteria,Verrucomicrobia,Actinobacteria,Spirochaetes,Chloroflexi,Deinococcus-Thermus,and Armatimonadetes.Furthermore,for the first time,there were representatives of the phyla Lentisphaerae found on paper machines.This study revealed the wide bacterial diversities of slime found on paper machines in China,which was also similar to other industrial processes.展开更多
Centromeres are chromosomal loci marked by histone variant Cen H3(centromeric histone H3)and essential for genomic stability and cell division.The budding yeast E3 ubiquitin ligase Psh1 selectively recognizes the yeas...Centromeres are chromosomal loci marked by histone variant Cen H3(centromeric histone H3)and essential for genomic stability and cell division.The budding yeast E3 ubiquitin ligase Psh1 selectively recognizes the yeast Cen H3(Cse4)for ubiquitination and controls the cellular level of Cse4 for proteolysis,but the underlying mechanism remains largely unknown.Here,we show that Psh1 uses a Cse4-binding domain(CBD,residues 1-211)to interact with Cse4-H4 instead of H3-H4,yielding a dissociation constant(Kd)of 27 nM.Psh1 recognizes Cse4-specific residues in the L1 loop and a2 helix to ensure Cse4 binding and ubiquitination.We map the Psh1-binding region of Cse4-H4 and identify a wide range of Cse4-specific residues required for the Psh1-mediated Cse4 recognition and ubiquitination.Further analyses reveal that histone chaperone Scm3 can impair Cse4 ubiquitination by abrogating Psh1-Cse4 binding.Together,our study reveals a novel Cse4-binding mode distinct from those of known Cen H3 chaperones and elucidates the mechanism by which Scm3 competes with Psh1 for Cse4 binding.展开更多
基金supported by grants from the Major Research Project of the Natural Science Foundation of Jiangsu Higher Education Institutions(No.14KJA53002)the Priority Academic Program Development of Jiangsu Higher Education Institutions(PAPD).
文摘Slime formation on paper machines is a critical issue that can substantially impact the quantity and quality of paper production.This problem is caused by the growth of an abundant and diverse amount of bacteria.Through the application of emulsion polymerase chain reaction(emPCR),the bacterial diversity was analyzed on paper machines and more operational taxonomic units(OTUs)were obtained.Eleven types of bacterial phyla were found that have been previously identified,including Proteobacteria(α-,β-,γ-,ε-,andφ-),Bacteroidetes,Firmicutes,Cyanobacteria,Verrucomicrobia,Actinobacteria,Spirochaetes,Chloroflexi,Deinococcus-Thermus,and Armatimonadetes.Furthermore,for the first time,there were representatives of the phyla Lentisphaerae found on paper machines.This study revealed the wide bacterial diversities of slime found on paper machines in China,which was also similar to other industrial processes.
基金supported by the grants from Natural Science Foundation of China(31521002,31970621,31871318,31671344,31801070)National Key Research and Development Program of China(2019YFA0508902)Strategic Priority Research Program(XDB37010100)。
文摘Centromeres are chromosomal loci marked by histone variant Cen H3(centromeric histone H3)and essential for genomic stability and cell division.The budding yeast E3 ubiquitin ligase Psh1 selectively recognizes the yeast Cen H3(Cse4)for ubiquitination and controls the cellular level of Cse4 for proteolysis,but the underlying mechanism remains largely unknown.Here,we show that Psh1 uses a Cse4-binding domain(CBD,residues 1-211)to interact with Cse4-H4 instead of H3-H4,yielding a dissociation constant(Kd)of 27 nM.Psh1 recognizes Cse4-specific residues in the L1 loop and a2 helix to ensure Cse4 binding and ubiquitination.We map the Psh1-binding region of Cse4-H4 and identify a wide range of Cse4-specific residues required for the Psh1-mediated Cse4 recognition and ubiquitination.Further analyses reveal that histone chaperone Scm3 can impair Cse4 ubiquitination by abrogating Psh1-Cse4 binding.Together,our study reveals a novel Cse4-binding mode distinct from those of known Cen H3 chaperones and elucidates the mechanism by which Scm3 competes with Psh1 for Cse4 binding.
