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Microprocessor complex

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</style><div role="note" class="hatnote navigation-not-searchable">This article is about the protein complex. For the computer processor, see <a href="Microprocessor" title="Microprocessor">Microprocessor</a>.</div>

The microprocessor complex is a <a href="Protein_complex" title="Protein complex">protein complex</a> involved in the early stages of processing <a href="MicroRNA" title="MicroRNA">microRNA</a> (miRNA) and <a href="RNA_interference" title="RNA interference">RNA interference</a> (RNAi) in animal cells.<a href="#cite_note-gregory-2">[2]</a><a href="#cite_note-denli-3">[3]</a> The complex is minimally composed of the <a href="Ribonuclease" title="Ribonuclease">ribonuclease</a> enzyme <a href="Drosha" title="Drosha">Drosha</a> and the dimeric <a href="RNA-binding_protein" title="RNA-binding protein">RNA-binding protein</a> <a href="DGCR8" class="mw-redirect" title="DGCR8">DGCR8</a> (also known as Pasha in non-human animals), and cleaves primary miRNA <a href="Substrate_(chemistry)" title="Substrate (chemistry)">substrates</a> to pre-miRNA in the <a href="Cell_nucleus" title="Cell nucleus">cell nucleus</a>.<a href="#cite_note-siomi-4">[4]</a><a href="#cite_note-wilson-5">[5]</a><a href="#cite_note-macias-6">[6]</a> Microprocessor is also the smaller of the two multi-protein complexes that contain human <a href="Drosha" title="Drosha">Drosha</a>.<a href="#cite_note-:0-7">[7]</a>

<div class="mw-heading mw-heading2"><h2 id="Composition">Composition</h2></div>

The microprocessor complex consists minimally of two proteins: <a href="Drosha" title="Drosha">Drosha</a>, a <a href="Ribonuclease_III" title="Ribonuclease III">ribonuclease III</a> enzyme; and <a href="DGCR8" class="mw-redirect" title="DGCR8">DGCR8</a>, a <a href="Double-stranded_RNA" title="Double-stranded RNA">double-stranded RNA</a> <a href="RNA-binding_protein" title="RNA-binding protein">binding protein</a>.<a href="#cite_note-siomi-4">[4]</a><a href="#cite_note-wilson-5">[5]</a><a href="#cite_note-macias-6">[6]</a> (DGCR8 is the name used in mammalian genetics, abbreviated from "<a href="DiGeorge_syndrome" title="DiGeorge syndrome">DiGeorge syndrome</a> critical region 8"; the homologous protein in <a href="Model_organism" title="Model organism">model organisms</a> such as <a href="Drosophila_melanogaster" title="Drosophila melanogaster">flies</a> and <a href="Caenorhabditis_elegans" title="Caenorhabditis elegans">worms</a> is called Pasha, for Partner of Drosha.) The <a href="Stoichiometry" title="Stoichiometry">stoichiometry</a> of the minimal complex was at one point experimentally difficult to determine, but it has been demonstrated to be a <a href="Protein_trimer" title="Protein trimer">heterotrimer</a> of two DGCR8 proteins and one Drosha.<a href="#cite_note-partin_2020-1">[1]</a><a href="#cite_note-kwon-8">[8]</a><a href="#cite_note-herbert-9">[9]</a><a href="#cite_note-nguyen-10">[10]</a>

In addition to the minimal catalytically active microprocessor components, other cofactors such as <a href="DEAD/DEAH_box_helicase" class="mw-redirect" title="DEAD/DEAH box helicase">DEAD box RNA helicases</a> and <a href="Heterogeneous_nuclear_ribonucleoprotein" class="mw-redirect" title="Heterogeneous nuclear ribonucleoprotein">heterogeneous nuclear ribonucleoproteins</a> may be present in the complex to mediate the activity of <a href="Drosha" title="Drosha">Drosha</a>.<a href="#cite_note-siomi-4">[4]</a> Some miRNAs are processed by microprocessor only in the presence of specific cofactors.<a href="#cite_note-ha-11">[11]</a>

<div class="mw-heading mw-heading2"><h2 id="Function">Function</h2></div>

Located in the <a href="Cell_nucleus" title="Cell nucleus">cell nucleus</a>, the microprocessor complex cleaves <a href="Primary_miRNA" class="mw-redirect" title="Primary miRNA">primary miRNA</a> (pri-miRNA) into <a href="Precursor_mRNA" class="mw-redirect" title="Precursor mRNA">precursor miRNA</a> (pre-miRNA).<a href="#cite_note-13">[13]</a> Its two subunits have been determined as necessary and sufficient for the mediation of the development of miRNAs from the pri-miRNAs.<a href="#cite_note-:0-7">[7]</a> These molecules of around 70 nucleotides contain a <a href="Stem-loop" title="Stem-loop">stem-loop</a> or hairpin structure. Pri-miRNA <a href="Substrate_(chemistry)" title="Substrate (chemistry)">substrates</a> can be derived either from <a href="Non-coding_RNA" title="Non-coding RNA">non-coding RNA</a> genes or from <a href="Intron" title="Intron">introns</a>. In the latter case, there is evidence that the microprocessor complex interacts with the <a href="Spliceosome" title="Spliceosome">spliceosome</a> and that the pri-miRNA processing occurs prior to <a href="RNA_splicing" title="RNA splicing">splicing</a>.<a href="#cite_note-wilson-5">[5]</a><a href="#cite_note-kataoka-14">[14]</a>

Microprocessor cleavage of pri-miRNAs typically occurs co-<a href="Transcription_(biology)" title="Transcription (biology)">transcriptionally</a> and leaves a characteristic RNase III <a href="Single-stranded" class="mw-redirect" title="Single-stranded">single-stranded</a> overhang of 2-3 nucleotides, which serves as a recognition element for the transport protein <a href="Exportin-5" class="mw-redirect" title="Exportin-5">exportin-5</a>.<a href="#cite_note-morlando-15">[15]</a> Pre-miRNAs are exported from the nucleus to the <a href="Cytoplasm" title="Cytoplasm">cytoplasm</a> in a <a href="RanGTP" class="mw-redirect" title="RanGTP">RanGTP</a>-dependent manner and are further processed, typically by the <a href="Endoribonuclease" title="Endoribonuclease">endoribonuclease</a> enzyme <a href="Dicer" title="Dicer">Dicer</a>.<a href="#cite_note-siomi-4">[4]</a><a href="#cite_note-wilson-5">[5]</a><a href="#cite_note-macias-6">[6]</a>

<a href="Hemin" title="Hemin">Hemin</a> allows for the increased processing of pri-miRNAs through an induced conformational change of the DGCR8 subunit, and also enhances DGCR8's binding specificity for RNA.<a href="#cite_note-16">[16]</a> <a href="Microprocessor_complex_subunit_DGCR8" title="Microprocessor complex subunit DGCR8">DGCR8</a> recognizes the junctions between hairpin structures and <a href="Single-stranded" class="mw-redirect" title="Single-stranded">single-stranded</a> RNA and serves to orient <a href="Drosha" title="Drosha">Drosha</a> to cleave around 11 <a href="Nucleotide" title="Nucleotide">nucleotides</a> away from the junctions, and remains in contact with the pri-miRNAs following cleavage and dissociation of Drosha.<a href="#cite_note-bellemer_2012-17">[17]</a>

Although the large majority of miRNAs undergo processing by microprocessor, a small number of exceptions called <a href="Mirtrons" class="mw-redirect" title="Mirtrons">mirtrons</a> have been described; these are very small introns which, after splicing, have the appropriate size and stem-loop structure to serve as a pre-miRNA.<a href="#cite_note-winter-18">[18]</a> The processing pathways for microRNA and for exogenously derived <a href="Small_interfering_RNA" title="Small interfering RNA">small interfering RNA</a> converge at the point of <a href="Dicer" title="Dicer">Dicer</a> processing and are largely identical downstream. Broadly defined, both pathways constitute <a href="RNA_interference" title="RNA interference">RNAi</a>.<a href="#cite_note-wilson-5">[5]</a><a href="#cite_note-winter-18">[18]</a> Microprocessor is also found to be involved in <a href="Ribosome_biogenesis" title="Ribosome biogenesis">ribosomal biogenesis</a> specifically in the removal of <a href="R-loop" title="R-loop">R-loops</a> and activating transcription of ribosomal protein encoding genes.<a href="#cite_note-19">[19]</a>

<div class="mw-heading mw-heading2"><h2 id="Regulation">Regulation</h2></div>

<a href="Gene_regulation" class="mw-redirect" title="Gene regulation">Gene regulation</a> by miRNA is widespread across many <a href="Genome" title="Genome">genomes</a> – by some estimates more than 60% of human protein-coding genes are likely to be regulated by miRNA,<a href="#cite_note-friedman-20">[20]</a> though the quality of experimental evidence for miRNA-target interactions is often weak.<a href="#cite_note-lee-21">[21]</a> Because processing by microprocessor is a major determinant of miRNA abundance, microprocessor itself is then an important target of regulation.

Both <a href="Drosha" title="Drosha">Drosha</a> and <a href="Microprocessor_complex_subunit_DGCR8" title="Microprocessor complex subunit DGCR8">DGCR8</a> are subject to regulation by <a href="Post-translational_modification" title="Post-translational modification">post-translational modifications</a> modulating stability, intracellular localization, and activity levels. Activity against particular substrates may be regulated by additional protein cofactors interacting with the microprocessor complex. The loop region of the pri-miRNA stem-loop is also a recognition element for regulatory proteins, which may up- or down-regulate microprocessor processing of the specific miRNAs they target.<a href="#cite_note-ha-11">[11]</a>

Microprocessor itself is auto-regulated by <a href="Negative_feedback" title="Negative feedback">negative feedback</a> through association with a pri-miRNA-like hairpin structure found in the <a href="Microprocessor_complex_subunit_DGCR8" title="Microprocessor complex subunit DGCR8">DGCR8</a> mRNA, which when cleaved reduces <a href="Microprocessor_complex_subunit_DGCR8" title="Microprocessor complex subunit DGCR8">DGCR8</a> expression. The structure in this case is located in an <a href="Exon" title="Exon">exon</a> and is unlikely to itself function as miRNA in its own right.<a href="#cite_note-ha-11">[11]</a>

<div class="mw-heading mw-heading2"><h2 id="Evolution">Evolution</h2></div>

<a href="Drosha" title="Drosha">Drosha</a> shares striking structural similarity with the downstream ribonuclease <a href="Dicer" title="Dicer">Dicer</a>, suggesting an evolutionary relationship, though <a href="Drosha" title="Drosha">Drosha</a> and related enzymes are found only in animals while Dicer relatives are widely distributed, including among <a href="Protozoan" class="mw-redirect" title="Protozoan">protozoans</a>.<a href="#cite_note-kwon-8">[8]</a> Both components of the microprocessor complex are <a href="Sequence_conservation" class="mw-redirect" title="Sequence conservation">conserved</a> among the vast majority of <a href="Metazoan" class="mw-redirect" title="Metazoan">metazoans</a> with known genomes. <a href="Mnemiopsis_leidyi" class="mw-redirect" title="Mnemiopsis leidyi">Mnemiopsis leidyi</a>, a <a href="Ctenophore" class="mw-redirect" title="Ctenophore">ctenophore</a>, lacks both <a href="Drosha" title="Drosha">Drosha</a> and <a href="Microprocessor_complex_subunit_DGCR8" title="Microprocessor complex subunit DGCR8">DGCR8</a> homologs, as well as recognizable miRNAs, and is the only known <a href="Metazoan" class="mw-redirect" title="Metazoan">metazoan</a> with no detectable genomic evidence of <a href="Drosha" title="Drosha">Drosha</a>.<a href="#cite_note-maxwell-22">[22]</a> In plants, the miRNA biogenesis pathway is somewhat different; neither Drosha nor DGCR8 has a <a href="Homology_(biology)" title="Homology (biology)">homolog</a> in plant cells, where the first step in miRNA processing is usually executed by a different <a href="Cell_nucleus" title="Cell nucleus">nuclear</a> <a href="Ribonuclease" title="Ribonuclease">ribonuclease</a>, <a href="DCL1" title="DCL1">DCL1</a>, a homolog of <a href="Dicer" title="Dicer">Dicer</a>.<a href="#cite_note-ha-11">[11]</a><a href="#cite_note-axtell-23">[23]</a>

It has been suggested based on <a href="Phylogenetic" class="mw-redirect" title="Phylogenetic">phylogenetic</a> analysis that the key components of <a href="RNA_interference" title="RNA interference">RNA interference</a> based on exogenous <a href="Substrate_(chemistry)" title="Substrate (chemistry)">substrates</a> were present in the ancestral <a href="Eukaryote" title="Eukaryote">eukaryote</a>, likely as an <a href="Immune" class="mw-redirect" title="Immune">immune</a> mechanism against <a href="Virus" title="Virus">viruses</a> and <a href="Transposable_element" title="Transposable element">transposable elements</a>. Elaboration of this pathway for miRNA-mediated gene regulation is thought to have evolved later.<a href="#cite_note-cerutti-24">[24]</a>

<div class="mw-heading mw-heading2"><h2 id="Clinical_significance">Clinical significance</h2></div>

The involvement of miRNAs in diseases has led scientists to become more interested in the role of additional protein complexes, like microprocessor, that have the ability to influence or modulate the function and expression of miRNAs.<a href="#cite_note-25">[25]</a> Microprocessor complex component, DGCR8, is affected through the <a href="Microdeletion" class="mw-redirect" title="Microdeletion">micro-deletion</a> of <a href="22q11.2" class="mw-redirect" title="22q11.2">22q11.2</a>, a small portion of <a href="Chromosome_22" title="Chromosome 22">chromosome 22</a>. This deletion causes irregular processing of miRNAs which leads to <a href="DiGeorge_syndrome" title="DiGeorge syndrome">DiGeorge Syndrome</a>.<a href="#cite_note-26">[26]</a>

<div class="mw-heading mw-heading2"><h2 id="References">References</h2></div>

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