Toolkit/promoter fusion
promoter fusion
Taxonomy: Mechanism Branch / Architecture. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
Promoter fusion is a reporter construct pattern used in Saccharomyces cerevisiae to assay cis-regulatory activity associated with CRY2 repression. In the cited 1995 study, promoter fusions were analyzed alongside CRY2-lacZ gene fusions to identify cis-acting elements involved in regulation of CRY2 expression.
Usefulness & Problems
Why this is useful
This construct pattern is useful for functionally testing whether promoter-proximal sequences contribute to gene regulation in yeast. In the cited work, it supported dissection of CRY2 regulatory control by enabling expression assays of promoter-linked reporter constructs.
Problem solved
It helps distinguish promoter-level cis-acting contributions to CRY2 repression from other regulatory determinants assayed with gene fusions. This addressed the problem of identifying which CRY2-linked sequences are involved in feedback repression in Saccharomyces cerevisiae.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Architecture: A reusable architecture pattern for arranging parts into an engineered system.
Techniques
Functional AssayTarget processes
No target processes tagged yet.
Implementation Constraints
The reported implementation context is Saccharomyces cerevisiae and involves promoter fusion reporter constructs assayed together with CRY2-lacZ gene fusions. The evidence does not provide construct architecture, vector system, selection markers, or assay conditions beyond expression-based analysis.
The supplied evidence does not specify the exact promoter fragment boundaries, reporter readout details, or quantitative performance of the promoter fusion constructs. Independent replication and use beyond the CRY2 regulatory context are not documented in the provided material.
Validation
Supporting Sources
Ranked Claims
In wild-type Saccharomyces cerevisiae cells, CRY1 and CRY2 are expressed at an approximately 10:1 ratio.
The Saccharomyces cerevisiae CRY1 and CRY2 genes, which encode ribosomal protein rp59, are expressed at a 10:1 ratio in wild-type cells.
In wild-type Saccharomyces cerevisiae cells, CRY1 and CRY2 are expressed at an approximately 10:1 ratio.
The Saccharomyces cerevisiae CRY1 and CRY2 genes, which encode ribosomal protein rp59, are expressed at a 10:1 ratio in wild-type cells.
In wild-type Saccharomyces cerevisiae cells, CRY1 and CRY2 are expressed at an approximately 10:1 ratio.
The Saccharomyces cerevisiae CRY1 and CRY2 genes, which encode ribosomal protein rp59, are expressed at a 10:1 ratio in wild-type cells.
In wild-type Saccharomyces cerevisiae cells, CRY1 and CRY2 are expressed at an approximately 10:1 ratio.
The Saccharomyces cerevisiae CRY1 and CRY2 genes, which encode ribosomal protein rp59, are expressed at a 10:1 ratio in wild-type cells.
In wild-type Saccharomyces cerevisiae cells, CRY1 and CRY2 are expressed at an approximately 10:1 ratio.
The Saccharomyces cerevisiae CRY1 and CRY2 genes, which encode ribosomal protein rp59, are expressed at a 10:1 ratio in wild-type cells.
In wild-type Saccharomyces cerevisiae cells, CRY1 and CRY2 are expressed at an approximately 10:1 ratio.
The Saccharomyces cerevisiae CRY1 and CRY2 genes, which encode ribosomal protein rp59, are expressed at a 10:1 ratio in wild-type cells.
In wild-type Saccharomyces cerevisiae cells, CRY1 and CRY2 are expressed at an approximately 10:1 ratio.
The Saccharomyces cerevisiae CRY1 and CRY2 genes, which encode ribosomal protein rp59, are expressed at a 10:1 ratio in wild-type cells.
Ribosomal protein 59 expressed from either CRY1 or CRY2 represses expression of CRY2 but not CRY1.
Ribosomal protein 59, expressed from either CRY1 or CRY2, represses expression of CRY2 but not CRY1.
Ribosomal protein 59 expressed from either CRY1 or CRY2 represses expression of CRY2 but not CRY1.
Ribosomal protein 59, expressed from either CRY1 or CRY2, represses expression of CRY2 but not CRY1.
Ribosomal protein 59 expressed from either CRY1 or CRY2 represses expression of CRY2 but not CRY1.
Ribosomal protein 59, expressed from either CRY1 or CRY2, represses expression of CRY2 but not CRY1.
Ribosomal protein 59 expressed from either CRY1 or CRY2 represses expression of CRY2 but not CRY1.
Ribosomal protein 59, expressed from either CRY1 or CRY2, represses expression of CRY2 but not CRY1.
Ribosomal protein 59 expressed from either CRY1 or CRY2 represses expression of CRY2 but not CRY1.
Ribosomal protein 59, expressed from either CRY1 or CRY2, represses expression of CRY2 but not CRY1.
Ribosomal protein 59 expressed from either CRY1 or CRY2 represses expression of CRY2 but not CRY1.
Ribosomal protein 59, expressed from either CRY1 or CRY2, represses expression of CRY2 but not CRY1.
Ribosomal protein 59 expressed from either CRY1 or CRY2 represses expression of CRY2 but not CRY1.
Ribosomal protein 59, expressed from either CRY1 or CRY2, represses expression of CRY2 but not CRY1.
Deletion or inactivation of CRY1 increases CRY2 mRNA levels by 5- to 10-fold.
Deletion or inactivation of CRY1 leads to 5- to 10-fold-increased levels of CRY2 mRNA.
Deletion or inactivation of CRY1 increases CRY2 mRNA levels by 5- to 10-fold.
Deletion or inactivation of CRY1 leads to 5- to 10-fold-increased levels of CRY2 mRNA.
Deletion or inactivation of CRY1 increases CRY2 mRNA levels by 5- to 10-fold.
Deletion or inactivation of CRY1 leads to 5- to 10-fold-increased levels of CRY2 mRNA.
Deletion or inactivation of CRY1 increases CRY2 mRNA levels by 5- to 10-fold.
Deletion or inactivation of CRY1 leads to 5- to 10-fold-increased levels of CRY2 mRNA.
Deletion or inactivation of CRY1 increases CRY2 mRNA levels by 5- to 10-fold.
Deletion or inactivation of CRY1 leads to 5- to 10-fold-increased levels of CRY2 mRNA.
Deletion or inactivation of CRY1 increases CRY2 mRNA levels by 5- to 10-fold.
Deletion or inactivation of CRY1 leads to 5- to 10-fold-increased levels of CRY2 mRNA.
Deletion or inactivation of CRY1 increases CRY2 mRNA levels by 5- to 10-fold.
Deletion or inactivation of CRY1 leads to 5- to 10-fold-increased levels of CRY2 mRNA.
The regulatory sequence of CRY2 is phylogenetically conserved, with a very similar sequence present at the 5' end of the RP59 gene in Kluyveromyces lactis.
The regulatory sequence of CRY2 is phylogenetically conserved; a very similar sequence is present in the 5' end of the RP59 gene of the yeast Kluyveromyces lactis.
The regulatory sequence of CRY2 is phylogenetically conserved, with a very similar sequence present at the 5' end of the RP59 gene in Kluyveromyces lactis.
The regulatory sequence of CRY2 is phylogenetically conserved; a very similar sequence is present in the 5' end of the RP59 gene of the yeast Kluyveromyces lactis.
The regulatory sequence of CRY2 is phylogenetically conserved, with a very similar sequence present at the 5' end of the RP59 gene in Kluyveromyces lactis.
The regulatory sequence of CRY2 is phylogenetically conserved; a very similar sequence is present in the 5' end of the RP59 gene of the yeast Kluyveromyces lactis.
The regulatory sequence of CRY2 is phylogenetically conserved, with a very similar sequence present at the 5' end of the RP59 gene in Kluyveromyces lactis.
The regulatory sequence of CRY2 is phylogenetically conserved; a very similar sequence is present in the 5' end of the RP59 gene of the yeast Kluyveromyces lactis.
The regulatory sequence of CRY2 is phylogenetically conserved, with a very similar sequence present at the 5' end of the RP59 gene in Kluyveromyces lactis.
The regulatory sequence of CRY2 is phylogenetically conserved; a very similar sequence is present in the 5' end of the RP59 gene of the yeast Kluyveromyces lactis.
The regulatory sequence of CRY2 is phylogenetically conserved, with a very similar sequence present at the 5' end of the RP59 gene in Kluyveromyces lactis.
The regulatory sequence of CRY2 is phylogenetically conserved; a very similar sequence is present in the 5' end of the RP59 gene of the yeast Kluyveromyces lactis.
The regulatory sequence of CRY2 is phylogenetically conserved, with a very similar sequence present at the 5' end of the RP59 gene in Kluyveromyces lactis.
The regulatory sequence of CRY2 is phylogenetically conserved; a very similar sequence is present in the 5' end of the RP59 gene of the yeast Kluyveromyces lactis.
Feedback regulation of CRY2 occurs posttranscriptionally.
Taken together, these results suggest that feedback regulation of CRY2 occurs posttranscriptionally.
Feedback regulation of CRY2 occurs posttranscriptionally.
Taken together, these results suggest that feedback regulation of CRY2 occurs posttranscriptionally.
Feedback regulation of CRY2 occurs posttranscriptionally.
Taken together, these results suggest that feedback regulation of CRY2 occurs posttranscriptionally.
Feedback regulation of CRY2 occurs posttranscriptionally.
Taken together, these results suggest that feedback regulation of CRY2 occurs posttranscriptionally.
Feedback regulation of CRY2 occurs posttranscriptionally.
Taken together, these results suggest that feedback regulation of CRY2 occurs posttranscriptionally.
Feedback regulation of CRY2 occurs posttranscriptionally.
Taken together, these results suggest that feedback regulation of CRY2 occurs posttranscriptionally.
Feedback regulation of CRY2 occurs posttranscriptionally.
Taken together, these results suggest that feedback regulation of CRY2 occurs posttranscriptionally.
CRY2 pre-mRNA accumulates in mtr mutants and upf1 mutants, suggesting that unspliced CRY2 pre-mRNA is degraded in the cytoplasm in wild-type repressed cells.
Increased levels of CRY2 pre-mRNA are present in mtr mutants, defective in mRNA transport, and in upf1 mutants, defective in degradation of cytoplasmic RNA, suggesting that in wild-type repressed cells, unspliced CRY2 pre-mRNA is degraded in the cytoplasm.
CRY2 pre-mRNA accumulates in mtr mutants and upf1 mutants, suggesting that unspliced CRY2 pre-mRNA is degraded in the cytoplasm in wild-type repressed cells.
Increased levels of CRY2 pre-mRNA are present in mtr mutants, defective in mRNA transport, and in upf1 mutants, defective in degradation of cytoplasmic RNA, suggesting that in wild-type repressed cells, unspliced CRY2 pre-mRNA is degraded in the cytoplasm.
CRY2 pre-mRNA accumulates in mtr mutants and upf1 mutants, suggesting that unspliced CRY2 pre-mRNA is degraded in the cytoplasm in wild-type repressed cells.
Increased levels of CRY2 pre-mRNA are present in mtr mutants, defective in mRNA transport, and in upf1 mutants, defective in degradation of cytoplasmic RNA, suggesting that in wild-type repressed cells, unspliced CRY2 pre-mRNA is degraded in the cytoplasm.
CRY2 pre-mRNA accumulates in mtr mutants and upf1 mutants, suggesting that unspliced CRY2 pre-mRNA is degraded in the cytoplasm in wild-type repressed cells.
Increased levels of CRY2 pre-mRNA are present in mtr mutants, defective in mRNA transport, and in upf1 mutants, defective in degradation of cytoplasmic RNA, suggesting that in wild-type repressed cells, unspliced CRY2 pre-mRNA is degraded in the cytoplasm.
CRY2 pre-mRNA accumulates in mtr mutants and upf1 mutants, suggesting that unspliced CRY2 pre-mRNA is degraded in the cytoplasm in wild-type repressed cells.
Increased levels of CRY2 pre-mRNA are present in mtr mutants, defective in mRNA transport, and in upf1 mutants, defective in degradation of cytoplasmic RNA, suggesting that in wild-type repressed cells, unspliced CRY2 pre-mRNA is degraded in the cytoplasm.
CRY2 pre-mRNA accumulates in mtr mutants and upf1 mutants, suggesting that unspliced CRY2 pre-mRNA is degraded in the cytoplasm in wild-type repressed cells.
Increased levels of CRY2 pre-mRNA are present in mtr mutants, defective in mRNA transport, and in upf1 mutants, defective in degradation of cytoplasmic RNA, suggesting that in wild-type repressed cells, unspliced CRY2 pre-mRNA is degraded in the cytoplasm.
CRY2 pre-mRNA accumulates in mtr mutants and upf1 mutants, suggesting that unspliced CRY2 pre-mRNA is degraded in the cytoplasm in wild-type repressed cells.
Increased levels of CRY2 pre-mRNA are present in mtr mutants, defective in mRNA transport, and in upf1 mutants, defective in degradation of cytoplasmic RNA, suggesting that in wild-type repressed cells, unspliced CRY2 pre-mRNA is degraded in the cytoplasm.
Sequences necessary and sufficient for regulation of CRY2 lie within the transcribed region, including the 5' exon and the first 62 nucleotides of the intron.
Sequences necessary and sufficient for regulation lie within the transcribed region of CRY2, including the 5' exon and the first 62 nucleotides of the intron.
Sequences necessary and sufficient for regulation of CRY2 lie within the transcribed region, including the 5' exon and the first 62 nucleotides of the intron.
Sequences necessary and sufficient for regulation lie within the transcribed region of CRY2, including the 5' exon and the first 62 nucleotides of the intron.
Sequences necessary and sufficient for regulation of CRY2 lie within the transcribed region, including the 5' exon and the first 62 nucleotides of the intron.
Sequences necessary and sufficient for regulation lie within the transcribed region of CRY2, including the 5' exon and the first 62 nucleotides of the intron.
Sequences necessary and sufficient for regulation of CRY2 lie within the transcribed region, including the 5' exon and the first 62 nucleotides of the intron.
Sequences necessary and sufficient for regulation lie within the transcribed region of CRY2, including the 5' exon and the first 62 nucleotides of the intron.
Sequences necessary and sufficient for regulation of CRY2 lie within the transcribed region, including the 5' exon and the first 62 nucleotides of the intron.
Sequences necessary and sufficient for regulation lie within the transcribed region of CRY2, including the 5' exon and the first 62 nucleotides of the intron.
Sequences necessary and sufficient for regulation of CRY2 lie within the transcribed region, including the 5' exon and the first 62 nucleotides of the intron.
Sequences necessary and sufficient for regulation lie within the transcribed region of CRY2, including the 5' exon and the first 62 nucleotides of the intron.
Sequences necessary and sufficient for regulation of CRY2 lie within the transcribed region, including the 5' exon and the first 62 nucleotides of the intron.
Sequences necessary and sufficient for regulation lie within the transcribed region of CRY2, including the 5' exon and the first 62 nucleotides of the intron.
Both the secondary structure and nucleotide sequence of the regulatory region of CRY2 pre-mRNA are necessary for repression.
Analysis of CRY2 point mutations corroborates these results and indicates that both the secondary structure and sequence of the regulatory region of CRY2 pre-mRNA are necessary for repression.
Both the secondary structure and nucleotide sequence of the regulatory region of CRY2 pre-mRNA are necessary for repression.
Analysis of CRY2 point mutations corroborates these results and indicates that both the secondary structure and sequence of the regulatory region of CRY2 pre-mRNA are necessary for repression.
Both the secondary structure and nucleotide sequence of the regulatory region of CRY2 pre-mRNA are necessary for repression.
Analysis of CRY2 point mutations corroborates these results and indicates that both the secondary structure and sequence of the regulatory region of CRY2 pre-mRNA are necessary for repression.
Both the secondary structure and nucleotide sequence of the regulatory region of CRY2 pre-mRNA are necessary for repression.
Analysis of CRY2 point mutations corroborates these results and indicates that both the secondary structure and sequence of the regulatory region of CRY2 pre-mRNA are necessary for repression.
Both the secondary structure and nucleotide sequence of the regulatory region of CRY2 pre-mRNA are necessary for repression.
Analysis of CRY2 point mutations corroborates these results and indicates that both the secondary structure and sequence of the regulatory region of CRY2 pre-mRNA are necessary for repression.
Both the secondary structure and nucleotide sequence of the regulatory region of CRY2 pre-mRNA are necessary for repression.
Analysis of CRY2 point mutations corroborates these results and indicates that both the secondary structure and sequence of the regulatory region of CRY2 pre-mRNA are necessary for repression.
Both the secondary structure and nucleotide sequence of the regulatory region of CRY2 pre-mRNA are necessary for repression.
Analysis of CRY2 point mutations corroborates these results and indicates that both the secondary structure and sequence of the regulatory region of CRY2 pre-mRNA are necessary for repression.
Approval Evidence
cis-Acting elements involved in repression of CRY2 were identified by assaying the expression of CRY2-lacZ gene fusions and promoter fusions
Source:
Sequences necessary and sufficient for regulation of CRY2 lie within the transcribed region, including the 5' exon and the first 62 nucleotides of the intron.
Sequences necessary and sufficient for regulation lie within the transcribed region of CRY2, including the 5' exon and the first 62 nucleotides of the intron.
Source:
Comparisons
Source-backed strengths
The evidence shows that promoter fusions were directly used to identify cis-acting elements involved in repression of CRY2. Their use in parallel with CRY2-lacZ gene fusions indicates a comparative reporter strategy for parsing regulatory sequence contributions.
Compared with CheRiff
promoter fusion and CheRiff address a similar problem space.
Shared frame: same top-level item type
Strengths here: looks easier to implement in practice.
Compared with intermolecular disulfide-based light switch
promoter fusion and intermolecular disulfide-based light switch address a similar problem space.
Shared frame: same top-level item type
Strengths here: looks easier to implement in practice.
promoter fusion and Pyr-NHS-functionalised 3D graphene foam electrode biosensor address a similar problem space.
Shared frame: same top-level item type
Ranked Citations
- 1.