c-mos Upstream sequence exhibits species-specific enhancer activity and binds murine-specific nuclear proteins

1987 ◽  
Vol 193 (2) ◽  
pp. 255-266 ◽  
Author(s):  
Frans A. van der Hoorn
Keyword(s):  
Nuclear Proteins ◽  
Upstream Sequence ◽  
Enhancer Activity ◽  
Species Specific

Sequence and spatial requirements for the tissue- and species-independent 3'-end processing mechanism of plant mRNA

1994 ◽  
Vol 14 (10) ◽  
pp. 6829-6838
Author(s):  
L Wu ◽  
T Ueda ◽  
J Messing
Keyword(s):  
Transcription Unit ◽  
Cauliflower Mosaic Virus ◽  
Upstream Region ◽  
General Mechanism ◽  
Upstream Sequence ◽  
Preference Order ◽  
Spatial Positioning ◽  
Species Specific ◽  
Zein Mrna ◽  
Processing Mechanism

Two cis-regulatory regions are required for efficient mRNA 3'-end processing of the maize 27-kDa zein mRNA: a region containing a duplicated AAUGAA poly(A) signal and a region that is present upstream from it. Strict spatial positioning of these two regions is required for efficient mRNA 3'-end processing. Insertion of a stuffer sequence as short as 17 or 18 bp either between the upstream region and the two AAUGAA motifs or between the two AAUGAA motifs drastically reduced the efficiency of 3'-end processing. Mutational analyses of the nucleotide preference at the fourth position of the AAUGAA motif revealed the preference order G > A >> C or U, suggesting that AAUAAA is neither a defective nor an optimal poly(A) signal for the 27-kDa zein mRNA. As for the 3' control region of the cauliflower mosaic virus (CaMV) transcription unit, the mRNA 3'-end processing mechanism mediated by the 27-kDa zein 3' control sequence is neither tissue nor species specific. The 3' upstream sequence of the 27-kDa zein gene can functionally replace that of the CaMV transcription unit. Conversely, the CaMV upstream sequence can mediate mRNA polyadenylation in the presence of a duplicated 27-kDa zein poly(A) signal. However, instead of the proximal poly(A) signal normally used in the 27-kDa zein mRNA, the distal signal is utilized. These results suggest that a general mechanism controls the 3'-end processing of plant mRNAs and that the cis-regulatory functions mediated by their upstream regions are interchangeable.

IMMUNOFLUORESCENT STUDIES OF BASIC NUCLEAR PROTEINS

1970 ◽  
Vol 12 (3) ◽  
pp. 570-581 ◽  
Author(s):  
L. A. David ◽  
Margaret J. Corey
Keyword(s):  
Nuclear Protein ◽  
Polytene Chromosomes ◽  
Nuclear Proteins ◽  
Root Tip ◽  
Salivary Gland Cells ◽  
Blood Smears ◽  
Calf Thymus ◽  
Species Specific ◽  
Phylogenetic Divergence ◽  
Tip Cells

Histone antibodies were obtained by injecting salt extracted calf thymus basic nuclear proteins into chickens. Fluorescent globulins were prepared from chicken antisera with precipitating antibodies against a single electrophoretic fraction of the nuclear protein extract. The fluorescent antiserum was specific for nuclei and chromosomes but was neither organ nor species specific. It reacted specifically with nuclei of cell imprints of bovine and human leucocytes, with polytene chromosomes from Chironomus salivary gland cells, and with nuclei from lily and onion root tip cells. It did not react with chicken blood smears. A decrease in the intensity of fluorescence roughly proportional to the phylogenetic divergence of the tested species was observed.These studies indicate that this basic nuclear protein fraction has acquired remarkably little variation over a long evolutionary period.

scholarly journals Allelic polymorphism in transcriptional regulatory regions of HLA-DQB genes.

1991 ◽  
Vol 173 (1) ◽  
pp. 181-192 ◽  
Author(s):  
L C Andersen ◽  
J S Beaty ◽  
J W Nettles ◽  
C E Seyfried ◽  
G T Nepom ◽  
...  
Keyword(s):  
Expression System ◽  
Regulatory Region ◽  
Class Ii ◽  
Nuclear Proteins ◽  
Nucleotide Sequencing ◽  
Upstream Sequence ◽  
Allelic Polymorphism ◽  
Sequence Element ◽  
Regulatory Regions ◽  
Allelic Differences

Class II genes of the human major histocompatibility complex (MHC) are highly polymorphic. Allelic variation of structural genes provides diversity in immune cell interactions, contributing to the formation of the T cell repertoire and to susceptibility to certain autoimmune diseases. We now report that allelic polymorphism also exists in the promoter and upstream regulatory regions (URR) of human histocompatibility leukocyte antigen (HLA) class II genes. Nucleotide sequencing of these regulatory regions of seven alleles of the DQB locus reveals a number of allele-specific polymorphisms, some of which lie in functionally critical consensus regions thought to be highly conserved in class II promoters. These sequence differences also correspond to allelic differences in binding of nuclear proteins to the URR. Fragments of the URR of two DQB alleles were analyzed for binding to nuclear proteins extracted from human B lymphoblastoid cell lines (B-LCL). Gel retardation assays showed substantially different banding patterns to the two promoters, including prominent variation in nuclear protein binding to the partially conserved X box regions and a novel upstream polymorphic sequence element. Comparison of these two polymorphic alleles in a transient expression system demonstrated a marked difference in their promoter strengths determined by relative abilities to initiate transcription of the chloramphenicol acetyltransferase reporter gene in human B-LCL. Shuttling of URR sequences between alleles showed that functional variation corresponded to both the X box and upstream sequence polymorphic sites. These findings identify an important source of MHC class II diversity, and suggest the possibility that such regulatory region polymorphisms may confer allelic differences in expression, inducibility, and/or tissue specificity of class II molecules.

scholarly journals Sequence and spatial requirements for the tissue- and species-independent 3'-end processing mechanism of plant mRNA.

1994 ◽  
Vol 14 (10) ◽  
pp. 6829-6838 ◽  
Author(s):  
L Wu ◽  
T Ueda ◽  
J Messing
Keyword(s):  
Transcription Unit ◽  
Cauliflower Mosaic Virus ◽  
Upstream Region ◽  
General Mechanism ◽  
Upstream Sequence ◽  
Preference Order ◽  
Spatial Positioning ◽  
Species Specific ◽  
Zein Mrna ◽  
Processing Mechanism

Two cis-regulatory regions are required for efficient mRNA 3'-end processing of the maize 27-kDa zein mRNA: a region containing a duplicated AAUGAA poly(A) signal and a region that is present upstream from it. Strict spatial positioning of these two regions is required for efficient mRNA 3'-end processing. Insertion of a stuffer sequence as short as 17 or 18 bp either between the upstream region and the two AAUGAA motifs or between the two AAUGAA motifs drastically reduced the efficiency of 3'-end processing. Mutational analyses of the nucleotide preference at the fourth position of the AAUGAA motif revealed the preference order G > A >> C or U, suggesting that AAUAAA is neither a defective nor an optimal poly(A) signal for the 27-kDa zein mRNA. As for the 3' control region of the cauliflower mosaic virus (CaMV) transcription unit, the mRNA 3'-end processing mechanism mediated by the 27-kDa zein 3' control sequence is neither tissue nor species specific. The 3' upstream sequence of the 27-kDa zein gene can functionally replace that of the CaMV transcription unit. Conversely, the CaMV upstream sequence can mediate mRNA polyadenylation in the presence of a duplicated 27-kDa zein poly(A) signal. However, instead of the proximal poly(A) signal normally used in the 27-kDa zein mRNA, the distal signal is utilized. These results suggest that a general mechanism controls the 3'-end processing of plant mRNAs and that the cis-regulatory functions mediated by their upstream regions are interchangeable.

scholarly journals The function of the nuclear envelope in nuclear protein accumulation.

1988 ◽  
Vol 106 (5) ◽  
pp. 1435-1444 ◽  
Author(s):  
F J Zimmer ◽  
C Dreyer ◽  
P Hausen
Keyword(s):  
Nuclear Envelope ◽  
Nuclear Protein ◽  
Specific Binding ◽  
Nuclear Proteins ◽  
Protein Accumulation ◽  
Nuclear Pores ◽  
Vegetal Pole ◽  
Immunohistochemical Methods ◽  
Species Specific ◽  
Host Nucleus

The mechanism by which proteins accumulate in the cell nucleus is not yet known. Two alternative mechanisms are discussed here: (a) selective unidirectional entry of karyophilic proteins through the nuclear pores, and (b) free diffusion of all proteins through the nuclear pores and specific binding of nuclear proteins to nondiffusible components of the nucleoplasm. We present experiments designed to distinguish between these alternatives. After mechanical injury of the Xenopus oocyte nuclear envelope, nuclear proteins were detected in the cytoplasm by immunohistochemical methods. In a second approach, nuclei from X. borealis oocytes were isolated under oil, the nuclear envelopes were removed, and the pure nucleoplasm was injected into the vegetal pole of X. laevis oocytes. With immunohistochemical methods, it was found that each of five nuclear proteins rapidly diffuses out of the injected nucleoplasm into the surrounding cytoplasm. The subsequent transport and accumulation in the intact host nucleus could be shown for the nuclear protein N1 with the aid of a species-specific mAb that reacts only with X. borealis N1. Purified and iodinated nucleoplasmin was injected into the cytoplasm of Xenopus oocytes and its uptake into the nucleus was studied by biochemical methods.

scholarly journals Differential activation of the mouse beta-globin promoter by enhancers.

1983 ◽  
Vol 3 (7) ◽  
pp. 1246-1254 ◽  
Author(s):  
P E Berg ◽  
J K Yu ◽  
Z Popovic ◽  
D Schumperli ◽  
H Johansen ◽  
...  
Keyword(s):  
Base Pair ◽  
Promoter Activity ◽  
Simian Virus 40 ◽  
Simian Virus ◽  
Beta Globin ◽  
Enhancer Activity ◽  
Sarcoma Virus ◽  
Mouse Cells ◽  
Globin Promoter ◽  
Species Specific

A series of plasmids was constructed to study the effect of two enhancers, the simian virus 40 72-base-pair repeat and the Harvey sarcoma virus 73-base-pair repeat, on the mouse beta maj-globin promoter. These plasmids contain the mouse beta maj-globin promoter linked to the Escherichia coli galK gene, thus allowing galactokinase enzyme activity to be used as a measure of promoter function. In CV-1 (primate) cells, it was found that an enhancer is required for optimal promoter activity and that the simian virus 40 (primate) enhancer increases galactokinase fourfold more than the Harvey sarcoma virus (mouse) enhancer. In L (mouse) cells, however, the Harvey sarcoma virus enhancer is 1.3-fold stronger than the simian virus 40 enhancer. These data support the hypothesis that enhancer activity can be species specific. Furthermore, when both enhancers are present on the same plasmid, their effect is additive on the beta-globin promoter whether the plasmid is in CV-1 cells or L cells.

Differential activation of the mouse beta-globin promoter by enhancers

1983 ◽  
Vol 3 (7) ◽  
pp. 1246-1254
Author(s):  
P E Berg ◽  
J K Yu ◽  
Z Popovic ◽  
D Schumperli ◽  
H Johansen ◽  
...  
Keyword(s):  
Base Pair ◽  
Promoter Activity ◽  
Simian Virus 40 ◽  
Simian Virus ◽  
Beta Globin ◽  
Enhancer Activity ◽  
Sarcoma Virus ◽  
Mouse Cells ◽  
Globin Promoter ◽  
Species Specific

A series of plasmids was constructed to study the effect of two enhancers, the simian virus 40 72-base-pair repeat and the Harvey sarcoma virus 73-base-pair repeat, on the mouse beta maj-globin promoter. These plasmids contain the mouse beta maj-globin promoter linked to the Escherichia coli galK gene, thus allowing galactokinase enzyme activity to be used as a measure of promoter function. In CV-1 (primate) cells, it was found that an enhancer is required for optimal promoter activity and that the simian virus 40 (primate) enhancer increases galactokinase fourfold more than the Harvey sarcoma virus (mouse) enhancer. In L (mouse) cells, however, the Harvey sarcoma virus enhancer is 1.3-fold stronger than the simian virus 40 enhancer. These data support the hypothesis that enhancer activity can be species specific. Furthermore, when both enhancers are present on the same plasmid, their effect is additive on the beta-globin promoter whether the plasmid is in CV-1 cells or L cells.

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