montecristo, mtc
a component of nuage in the germline that functions to repress selfish genetic elements - Aub and Ago3 are recruited to nuage to form a ping-pong complex assembled by Krimper - simultaneously binds the N-terminal regions of Aub and Ago3 to promote generation of new piRNA - Krimper enforces an antisense bias on piRNA pools by binding AGO3 in the Drosophila germline
Please see the JBrowse view of Dmel\krimp for information on other features
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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 5.50
There is only one protein coding transcript and one polypeptide associated with this gene
Homooligomerizes (via N-terminus) (PubMed:26295961). Component of the ping-pong piRNA processing (4P) complex consisting of krimp, aub and AGO3; a single molecule of krimp can bind both aub and AGO3 without the need for homooligomerization (PubMed:26295961, PubMed:34210982). Interacts (via canonical tudor domain) with aub (via N-terminus when symmetrically dimethylated on arginine residues) (PubMed:26295961, PubMed:34210982). Interacts (via non-canonical tudor domain) with AGO3 (via N-terminus when unmethylated on arginine residues); this interaction leads to symmetrical dimethylation on AGO3 arginine residues and its subsequent dissociation from krimp (PubMed:26212455, PubMed:26295961, PubMed:34210982). Krimp associated AGO3 is mostly free of piRNA binding and the interaction plays an important role in the loading of AGO3 with piRNAs; piRNA binding stimulates methylation of ACO3 by the csul/PRMT5 methylosome complex and promotes dissociation of the two proteins (PubMed:26212455, PubMed:26295961, PubMed:34210982).
Possesses two tudor domains, a C-terminal canonical tudor domain and a central non-canonical tudor domain (Probable) (PubMed:34210982). Both tudor domains can interact with Piwi proteins allowing the simultaneous binding of aub and AGO3; this brings them in close proximity to facilitate their role in ping-pong ampification of piRNAs (PubMed:26295961, PubMed:34210982). The canonical tudor domain possesses a hydrophobic pocket that preferentially binds methylated aub; the interaction requires symmetrical methylation on at least one aub N-terminal arginine (PubMed:26295961, PubMed:34210982). The non-canonical tudor domain possesses a hydrophilic binding pocket that preferentially binds unmethylated AGO3; methylation on any of the AGO3 N-terminal arginines disrupts this interaction (PubMed:34210982). The differential binding preference ensures recruitment of one piRNA loaded (aub) and one unloaded (AGO3) Piwi-protein; the methylation state of the Piwi proteins acts as an indicator of their piRNA binding state (PubMed:34210982).
Click to get a list of regulatory features (enhancers, TFBS, etc.) and gene disruptions (point mutations, indels, etc.) within or overlapping Dmel\krimp 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).
Comment: maternally deposited
JBrowse - Visual display of RNA-Seq signals
View Dmel\krimp in JBrowse2-79
2-81.9
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.
polyclonal
monoclonal
Source for identity of: mtc CG15707
Source for identity of: krimp CG15707
The gene is named "montecristo", after a brand of Cuban cigars, due to the mutant eggshell phenotype.