scholarly journals Molecular characterization of hNRP, a cDNA encoding a human nucleosome-assembly-protein-I-related gene product involved in the induction of cell proliferation

1994 ◽  
Vol 297 (2) ◽  
pp. 389-397 ◽  
Author(s):  
H U Simon ◽  
G B Mills ◽  
M Kozlowski ◽  
D Hogg ◽  
D Branch ◽  
...  
Keyword(s):  
Cell Proliferation ◽  
Amino Acid ◽  
Gene Product ◽  
Thymidine Incorporation ◽  
Structural Features ◽  
Nucleosome Assembly ◽  
Proliferating Cells ◽  
Amino Acid Similarity ◽  
Nucleosome Assembly Protein

We have isolated from a human thymus cDNA library a cDNA clone encoding a potential protein with 54% amino acid similarity to that encoded by a previously identified cDNA for yeast nucleosome assembly protein I (NAP-I). The deduced amino acid sequence for this newly identified cDNA, designated hNRP (human NAP-related protein), contains a potential seven-residue nuclear localization motif, three clusters of highly acidic residues and other structural features found in various proteins implicated in chromatin formation. When expressed as a fusion protein in Escherichia coli, hNRP reacted specifically with a monoclonal antibody raised against human NAP-I. The hNRP transcript was detected in all tissues and cell lines studied, but levels were somewhat increased in rapidly proliferating cells. Moreover, levels of both hNRP mRNA and protein increased rapidly in cultured T-lymphocytes induced to proliferate by incubation with phorbol ester and ionomycin. Phorbol 12-myristate 13-acetate/ionomycin-induced increases in both hNRP mRNA and mitogenesis, as measured by thymidine incorporation, were markedly inhibited, however, in cells treated with an hNRP antisense oligonucleotide. These results demonstrate a correlation between induction of hNRP expression and mitogenesis and taken together with the structural similarities between hNRP and yeast NAP-I suggest that the hNRP gene product participates in DNA replication and thereby plays an important role in the process of cell proliferation.

scholarly journals Crucial Role for Mst1 and Mst2 Kinases in Early Embryonic Development of the Mouse

2009 ◽  
Vol 29 (23) ◽  
pp. 6309-6320 ◽  
Author(s):  
Sangphil Oh ◽  
Dongjun Lee ◽  
Tackhoon Kim ◽  
Tae-Shin Kim ◽  
Hyun Jung Oh ◽  
...  
Keyword(s):  
Cell Proliferation ◽  
Single Copy ◽  
Mutant Mice ◽  
Placental Development ◽  
Mouse Development ◽  
Proliferating Cells ◽  
Vascular Patterning ◽  
Primitive Hematopoiesis ◽  
Early Mouse

ABSTRACT Mammalian sterile 20-like kinases 1 and 2 (Mst1 and Mst2, respectively) are potent serine/threonine kinases that are involved in cell proliferation and cell death. To investigate the physiological functions of Mst1 and Mst2, we generated Mst1 and Mst2 mutant mice. Mst1 −/− and Mst2 −/− mice were viable and fertile and developed normally, suggesting possible functional overlaps between the two genes. A characterization of heterozygous and homozygous combinations of Mst1 and Mst2 mutant mice showed that mice containing a single copy of either gene underwent normal organ development; however, Mst1 −/−; Mst2 −/− mice lacking both Mst1 and Mst2 genes started dying in utero at approximately embryonic day 8.5. Mst1 −/−; Mst2 −/− mice exhibited severe growth retardation, failed placental development, impaired yolk sac/embryo vascular patterning and primitive hematopoiesis, increased apoptosis in placentas and embryos, and disorganized proliferating cells in the embryo proper. These findings indicate that both Mst1 and Mst2 kinases play essential roles in early mouse development, regulating placental development, vascular patterning, primitive hematopoiesis, and cell proliferation and survival.

scholarly journals Cloning of the Novel Gene Encoding β-Agarase C from a Marine Bacterium, Vibrio sp. Strain PO-303, and Characterization of the Gene Product

2006 ◽  
Vol 72 (9) ◽  
pp. 6399-6401 ◽  
Author(s):  
Jinhua Dong ◽  
Shinnosuke Hashikawa ◽  
Takafumi Konishi ◽  
Yutaka Tamaru ◽  
Toshiyoshi Araki
Keyword(s):  
Amino Acid ◽  
Gene Product ◽  
Glycoside Hydrolase ◽  
Marine Bacterium ◽  
Glycoside Hydrolase Family ◽  
The Novel ◽  
Amino Acid Residues ◽  
Gene Encoding ◽  
Hydrolase Family

ABSTRACT The β-agarase C gene (agaC) of a marine bacterium, Vibrio sp. strain PO-303, consisted of 1,437 bp encoding 478 amino acid residues. β-Agarase C was identified as the first β-agarase that cannot hydrolyze neoagarooctaose and smaller neoagarooligosaccharides and was assigned to a novel glycoside hydrolase family.

scholarly journals Can, a putative oncogene associated with myeloid leukemogenesis, may be activated by fusion of its 3' half to different genes: characterization of the set gene.

1992 ◽  
Vol 12 (8) ◽  
pp. 3346-3355 ◽  
Author(s):  
M von Lindern ◽  
S van Baal ◽  
J Wiegant ◽  
A Raap ◽  
A Hagemeijer ◽  
...  
Keyword(s):  
Fusion Gene ◽  
Alternative Polyadenylation ◽  
Open Reading Frame ◽  
Sequence Motif ◽  
Nucleosome Assembly ◽  
Reading Frame ◽  
Nucleosome Assembly Protein ◽  
Gene Translocation ◽  
Translocation Breakpoints

The translocation (6;9)(p23;q34) in acute nonlymphocytic leukemia results in the formation of a highly consistent dek-can fusion gene. Translocation breakpoints invariably occur in single introns of dek and can, which were named icb-6 and icb-9, respectively. In a case of acute undifferentiated leukemia, a breakpoint was detected in icb-9 of can, whereas no breakpoint could be detected in dek. Genomic and cDNA cloning showed that instead of dek, a different gene was fused to can, which was named set. set encodes transcripts of 2.0 and 2.7 kb that result from the use of alternative polyadenylation sites. Both transcripts contain the open reading frame for a putative SET protein with a predicted molecular mass of 32 kDa. The set-can fusion gene is transcribed into a 5-kb transcript that contains a single open reading frame predicting a 155-kDa chimeric SET-CAN protein. The SET sequence shows homology with the yeast nucleosome assembly protein NAP-I. The only common sequence motif of SET and DEK proteins is an acidic region. SET has a long acidic tail, of which a large part is present in the predicted SET-CAN fusion protein. The set gene is located on chromosome 9q34, centromeric of c-abl. Since a dek-can fusion gene is present in t(6;9) acute myeloid leukemia and a set-can fusion gene was found in a case of acute undifferentiated leukemia, we assume that can may function as an oncogene activated by fusion of its 3' part to dek, set, or perhaps other genes.

Molecular cloning and functional characterization of a cDNA encoding nucleosome assembly protein 1 (NAP-1) from soybean

1995 ◽  
Vol 249 (5) ◽  
pp. 465-473 ◽  
Author(s):  
Hae Won Yoon ◽  
Min Chul Kim ◽  
Sang Yeoul Lee ◽  
Inhwan Hwang ◽  
Jeong Dong Bahk ◽  
...  
Keyword(s):  
Molecular Cloning ◽  
Functional Characterization ◽  
Nucleosome Assembly ◽  
Nucleosome Assembly Protein ◽  
Nucleosome Assembly Protein 1

Characterization of Caenorhabditis elegans Nucleosome Assembly Protein 1 Uncovers the Role of Acidic Tails in Histone Binding

Biochemistry ◽  
2018 ◽  
Vol 58 (2) ◽  
pp. 108-113 ◽  
Author(s):  
Prithwijit Sarkar ◽  
Naifu Zhang ◽  
Sudipta Bhattacharyya ◽  
Karlah Salvador ◽  
Sheena D’Arcy
Keyword(s):  
Caenorhabditis Elegans ◽  
Nucleosome Assembly ◽  
Histone Binding ◽  
Nucleosome Assembly Protein ◽  
Nucleosome Assembly Protein 1

scholarly journals Cell Proliferation and DNA Synthesis in Organizing White Mural Non-Occlusive Aortic Thrombus in Rabbits

1977 ◽  
Author(s):  
J. Rabinovitch ◽  
B.I. Weigensberg ◽  
R.H. More ◽  
A. Gotlieb
Keyword(s):  
Cell Proliferation ◽  
Polymorphonuclear Leukocytes ◽  
Thymidine Incorporation ◽  
Dry Weight ◽  
Variable Ratio ◽  
Proliferating Cells ◽  
Time Intervals ◽  
Dna Concentration ◽  
Aortic Thrombus ◽  
Very High

White mural non-occlusive thrombus induced experimentally in the aortae of rabbits contains appreciable numbers of proliferating cells which contribute bulk and mass to the lesion. As these cells proliferate they produce appreciable amounts of collagen, elastin, and mucopolysaccharide which make the lesions resistant to dissolution by enzymes. In this study the proliferation of cells was monitored at serial time intervals up to 60 weeks by radioautography and chemical measurement of [H3]thymidine incorporation into DNA in order to determine over what time intervals appropriate antiproliferative drugs might be tested to arrest the growth of these cells. DPM [H3 thymidine incorporation into DNA became significant on Day 2, remained very high until Day 14 and then declined. The concentration of DNA per mg delipidated dry weight of thrombus between Day 0 and 4 was highly variable (6 to 60 μg/mg) due to the highly variable ratio of nucleated cells (monocytes and polymorphonuclear leukocytes) to fibrin and platelets. Between Day 0 and 4 weeks the DNA concentration became less variable as the polymorphsand monocytes were replaced by macrophages and spindle-shaped cells (10 to 20 yg/DNA per mg delipidated lesion). After 4 weeks DNA concentration declined continuously until by 60 weeks there was 2 ± 1 μg DNA/mg delipidated dry weight of lesion as it was diluted by collagen, elastin, and mucopolysaccharide. It is concluded that if antiproliferative drugs are to be used, they must be started as early as Day 2 and be maintained for at least 2 weeks.

scholarly journals Bacterial lipolytic enzymes: classification and properties

1999 ◽  
Vol 343 (1) ◽  
pp. 177-183 ◽  
Author(s):  
Jean Louis ARPIGNY ◽  
Karl-Erich JAEGER
Keyword(s):  
Amino Acid ◽  
Structural Features ◽  
Biological Properties ◽  
Amino Acid Sequences ◽  
Important Class ◽  
Lipolytic Enzymes ◽  
Disulphide Bonds ◽  
Enzyme Families

Knowledge of bacterial lipolytic enzymes is increasing at a rapid and exciting rate. To obtain an overview of this industrially very important class of enzymes and their characteristics, we have collected and classified the information available from protein and nucleotide databases. Here we propose an updated and extensive classification of bacterial esterases and lipases based mainly on a comparison of their amino acid sequences and some fundamental biological properties. These new insights result in the identification of eight different families with the largest being further divided into six subfamilies. Moreover, the classification enables us to predict (1) important structural features such as residues forming the catalytic site or the presence of disulphide bonds, (2) types of secretion mechanism and requirement for lipase-specific foldases, and (3) the potential relationship to other enzyme families. This work will therefore contribute to a faster identification and to an easier characterization of novel bacterial lipolytic enzymes.

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