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FB2026_01
,
released March 12, 2026
novel myristoylprotein with a cluster of basic amino acids present in the basal junction and required for its formation at the onset of cellularization
Please see the JBrowse view of Dmel\nullo for information on other features
To submit a correction to a gene model please use the Contact FlyBase form
AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100. Some regions with low pLDDT may be unstructured in isolation.
Gene model reviewed during 5.52
1.0 (unknown)
There is only one protein coding transcript and one polypeptide associated with this gene
26.5, 25 (kD observed)
123 (aa)
Click to get a list of regulatory features (enhancers, TFBS, etc.) and gene disruptions (point mutations, indels, etc.) within or overlapping Dmel\nullo using the Feature Mapper tool.
The testis specificity index was calculated from modENCODE tissue expression data by Vedelek et al., 2018 to indicate the degree of testis enrichment compared to other tissues. Scores range from -2.52 (underrepresented) to 5.2 (very high testis bias).
nullo transcripts are first detected at embryonic cycle 11, peak during the mitosis separating cycles 13 and 14, and disappear rapidly at the beginning of cellularization. Expression occurs throughout the cortex of the embryo with less RNA accumulation at the poles than in the rest of the embryo. In cycle 14 broad bands of heavier accumulation are visible. Transcript levels in cycle 14 may be coupled to the nucleocytoplasmic ratio. nullo is not expressed at any other times in development. The onset of expression is not affected in Sry-α mutants and does not require any other zygotically acting genes.
nullo protein is blastoderm-specific and is detected between interphase of embryonic cycle 13 and the beginning of gastrulation, with highest levels in cycle 14 and during the slow phase of cellularization. nullo protein localizes between interphase actin caps and within metaphase furrows during cycle 13. At cycle 14, nullo protein co-localizes with the actin network in a punctate hexagonal pattern, and during the slow phase of cellularization continues to be associated with the plasma membrane at, and apical to, the invaginating furrow canal. During the fast phase, less protein is found at the furrow canal, and the majority of nullo protein is dispersed in the cytoplasm. Protein is not detected above background levels at the completion of cellularization.
JBrowse - Visual display of RNA-Seq signals
View Dmel\nullo in JBrowse1-19
1-20.4
Please Note FlyBase no longer curates genomic clone accessions so this list may not be complete
Please Note This section lists cDNAs and ESTs that fall within the genomic extent of the gene model, which may include cDNAs and ESTs of genes within introns, or of overlapping genes. Please see JBrowse for alignment of the cDNAs and ESTs to the gene model.
For each fully sequenced cDNA the DGRC maintains various forms of the cDNA (e.g tagged or untagged) in several different host vectors for subsequent cloning and expression in Drosophila and Drosophila cell lines.
monoclonal
dsRNA has been made from templates generated with primers directed against this gene.
dsRNA made from templates generated with primers directed against this gene is tested in an RNAi screen for effects on actin-based lamella formation.
nullo loss of function mutations cause defects in the formation and maintenance of the basal junction, but do not affect apical junction formation during cellularisation in the embryo.
In a sample of 79 genes with multiple introns, 33 showed significant heterogeneity in G+C content among introns of the same gene and significant positive correspondence between the intron and the third codon position G+C content within genes. These results are consistent with selection adding against preferred codons at the start of genes.
Introduction of Dvir\nullo into D.melanogaster nullo mutant embryos rescues the defects in the actin network and allows the development of viable adults.
P element constructs carrying a 4.5kb fragment containing nullo+t4.5 were able to rescue the embryonic lethality associated with nullo mutations.
The requirement for nullo function during development has been determined. Analysis of nullo mutant clones in adults reveals that nullo activity is not required for cell division in imaginal discs. Germline clone experiments suggest that maternal expression of nullo is not essential for either germline proliferation or the cellularisation of progeny.
The nullo gene is required for the stability of the actin-myosin contractile network during cellularization.
Source for merge of: nullo BcDNA:RE47733
Source for merge of nullo BcDNA:RE47733 was a shared cDNA ( date:030728 ).