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Biology subjects

Miller, T. C. R.

Publications and source records attributed to Miller, T. C. R..

4 recordsLinked to original sources

CRISPR-PTM and CRISPR-VEIS: Multiplexed platforms for quantitative functional analysis of endogenous phosphosites

Connecting protein post-translational modifications (PTMs) to phenotypic outcomes is a central challenge. Although phosphoproteomics has richly catalogued specific sites, reliable methods to measure the endogenous effects of individual phosphosites on cellular fitness and signaling are still lacking. Here, we introduce CRISPR-PTM and CRISPR-VEIS as complementary platforms for quantitative, endogenous phosphosite interrogation at both individual and clustered phosphorylation events. CRISPR-PTM is a multiplexed knock-in framework generating defined phosphosite variants with internal allelic markers, enabling precise relative fitness effects in pooled populations. CRISPR-VEIS (Visualisation of Edits In Situ) is an in situ mRNA-genotyping approach that directly links endogenous allelic edits to single-cell phenotypes, addressing needs for subclonal isolation or exogenous reporters. We applied these methods to the WEE1-CDK1 regulatory pathway, where canonical CDK1-Y15 phosphorylation alone cannot explain WEE1 loss or inhibition phenotypes. CRISPR-PTM systematically quantified fitness consequences of CDK1 phosphosite variants and identified Y19 as a previously unrecognized WEE1-dependent inhibitory site. Single non-phosphorylatable substitutions at Y15 or Y19 had minimal impact, but combined CDK1-Y15F/Y19F editing caused pronounced fitness defects, phenocopying WEE1 inactivation and showing epistasis to WEE1 inhibitors. CRISPR-VEIS further demonstrated that acute endogenous editing of both sites correlated with elevated CDK activity at the single-cell level. Together, CRISPR-PTM and CRISPR-VEIS provide broadly applicable approaches for quantitative analysis of PTM function, enabling direct linkage of endogenous phosphosite variation to cellular fitness and signaling phenotypes.

cell biology↗

SCAF1 driven polyadenylation site usage regulates mRNA isoform expression and neuronal differentiation

Accurate co-transcriptional processing is required for correct gene expression of mRNA transcript isoforms under unperturbed conditions, but particularly during development, to ensure tissue-specific mRNA isoform expression. Here we show that the poorly studied SR-related CTD-associated factors SCAF1 protein regulates polyadenylation site usage towards the end of genes. SCAF1 interacts directly with the phosphorylated C-terminal domain (CTD) of RNA polymerase II (RNAPII), in a complex enriched with elongation and 3 end processing factors. While SCAF1 knockout in HEK293 cells is innocuous, it leads to a shift towards expression of shorter mRNA transcripts by co-transcriptional usage of early polyadenylation sites. SCAF1 deficiency induced via auxin-dependent degradation in neuron differentiating mouse embryonic stem cells (mESCs) results in neuronal commitment defects, mediated by altered mRNA isoform usage that impacts expression of key neuronal genes. These findings highlight the importance of mRNA isoform usage and underscores the key role for SCAF proteins in its regulation though polyadenylation site selection.

molecular biology↗

MCM Double Hexamer Loading Visualised with Human Proteins

Eukaryotic DNA replication begins with the loading of the MCM replicative DNA helicase as a head-to-head double hexamer (DH) at origins of DNA replication1-3. Our current understanding of how DH is assembled by the Origin Recognition Complex (ORC), CDC6 and CDT1 comes mostly from budding yeast. Here we characterise human DH (hDH) loading using biochemical reconstitution and cryo-electron microscopy with purified proteins. We show that hDH engages DNA differently from yeast (yDH), and generates [~]5 base pairs of unwound DNA at the interface between hexamers, as seen in hDH isolated from cells4. We identify several differences from yeast in the order of factor recruitment and dependencies during hDH assembly. Unlike yeast5-8, the ORC6 subunit of ORC is not essential for initial MCM recruitment or hDH loading, but contributes to an alternative hDH assembly pathway requiring an intrinsically disordered region (IDR) in ORC1, which may work through a novel MCM-ORC (hMO*) intermediate. Our work presents a detailed view of how DHs are assembled in an organism utilising sequence-independent replication origins, it provides further evidence for diversity in eukaryotic DH assembly mechanisms9, and it represents the first step toward reconstitution of DNA replication initiation with purified human proteins.

biochemistry↗

Catalytic and non-catalytic functions of DNA polymerase kappa in translesion DNA synthesis

Translesion DNA synthesis (TLS) is an essential process that allows cells to bypass lesions encountered during DNA replication and is emerging as a primary target of chemotherapy. Among vertebrate DNA polymerases, polymerase kappa (Pol() has the unique ability to bypass minor groove DNA adducts in vitro. However, Pol(is also required for cells to overcome major groove DNA adducts but the basis of this requirement is unclear. Here, we combine CRISPR base editor screening technology in human cells with TLS analysis of defined DNA lesions in Xenopus egg extracts to unravel the functions and regulations of Pol(during lesion bypass. Strikingly, we show that Pol(has two main functions during TLS, which are differentially regulated via Rev1 binding. On the one hand, Pol(is essential to replicate across minor groove DNA lesions in a process that depends on PCNA ubiquitylation but is independent of Rev1. On the other hand, via its cooperative interaction with Rev1 and ubiquitylated PCNA, Pol(stabilizes the Rev1-Pol(extension complex on DNA to allow extension past major groove DNA lesions and abasic sites, in a process that is independent of Pol(catalytic activity. Together, our work identifies catalytic and non-catalytic functions of Pol(in TLS and reveals important regulatory mechanisms underlying the unique domain architecture present at the C-terminal end of Y-family TLS polymerases.

molecular biology↗