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Article ; Online: In conversation with Lori Passmore.

Dhillon, Paraminder / Skourti, Eleni / Passmore, Lori A

2023 Volume 290, Issue 20, Page(s) 4814–4819

Abstract: Lori Passmore is a Group Leader at the MRC Laboratory of Molecular Biology (MRC-LMB). She studied ... for a PhD at the Institute of Cancer Research. After completing her PhD, Lori moved to Cambridge ... where she became a Post-Doctoral Fellow at the MRC-LMB. In 2009, Lori started her own group at the MRC-LMB and was ...

Abstract	Lori Passmore is a Group Leader at the MRC Laboratory of Molecular Biology (MRC-LMB). She studied Biochemistry at the University of British Columbia in Vancouver (Canada), before moving to the UK in 1999 for a PhD at the Institute of Cancer Research. After completing her PhD, Lori moved to Cambridge, where she became a Post-Doctoral Fellow at the MRC-LMB. In 2009, Lori started her own group at the MRC-LMB and was subsequently awarded an ERC Starting Grant (2011), an ERC Consolidator Grant (2017) and a Wellcome Discovery Award (2023). She was also elected into the EMBO Young Investigator Programme (2015) and EMBO Membership (2018). Lori's research focusses on the determination of the structures of protein complexes that regulate gene expression, using primarily cryo-electron microscopy and in vitro assays. Her work has contributed significantly to our understanding of the underlying molecular mechanisms of cellular processes, giving insights into human physiology and disease. In this interview, Lori provides an overview of her research and discusses current challenges in the field, recalls the key events and collaborations that have helped shape her successful research career and offers advice to early career scientists.
MeSH term(s)	Female ; Humans ; Awards and Prizes ; Cryoelectron Microscopy ; Molecular Biology ; Neoplasms ; Research Personnel
Language	English
Publishing date	2023-05-03
Publishing country	England
Document type	Editorial ; Interview
ZDB-ID	2173655-8
ISSN	1742-4658 ; 1742-464X
ISSN (online)	1742-4658
ISSN	1742-464X
DOI	10.1111/febs.16782
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Article ; Online: 3'-End Processing of Eukaryotic mRNA: Machinery, Regulation, and Impact on Gene Expression.

Boreikaitė, Vytautė / Passmore, Lori A

Annual review of biochemistry

2023 Volume 92, Page(s) 199–225

Abstract: Formation of the 3' end of a eukaryotic mRNA is a key step in the production of a mature transcript. This process is mediated by a number of protein factors that cleave the pre-mRNA, add a poly(A) tail, and regulate transcription by protein ... ...

Abstract	Formation of the 3' end of a eukaryotic mRNA is a key step in the production of a mature transcript. This process is mediated by a number of protein factors that cleave the pre-mRNA, add a poly(A) tail, and regulate transcription by protein dephosphorylation. Cleavage and polyadenylation specificity factor (CPSF) in humans, or cleavage and polyadenylation factor (CPF) in yeast, coordinates these enzymatic activities with each other, with RNA recognition, and with transcription. The site of pre-mRNA cleavage can strongly influence the translation, stability, and localization of the mRNA. Hence, cleavage site selection is highly regulated. The length of the poly(A) tail is also controlled to ensure that every transcript has a similar tail when it is exported from the nucleus. In this review, we summarize new mechanistic insights into mRNA 3'-end processing obtained through structural studies and biochemical reconstitution and outline outstanding questions in the field.
MeSH term(s)	Humans ; RNA, Messenger/genetics ; RNA, Messenger/metabolism ; RNA Precursors/genetics ; RNA Precursors/metabolism ; mRNA Cleavage and Polyadenylation Factors/genetics ; mRNA Cleavage and Polyadenylation Factors/metabolism ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Gene Expression
Chemical Substances	RNA, Messenger ; RNA Precursors ; mRNA Cleavage and Polyadenylation Factors
Language	English
Publishing date	2023-03-31
Publishing country	United States
Document type	Journal Article ; Review ; Research Support, Non-U.S. Gov't
ZDB-ID	207924-0
ISSN	1545-4509 ; 0066-4154
ISSN (online)	1545-4509
ISSN	0066-4154
DOI	10.1146/annurev-biochem-052521-012445
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Article ; Online: Knowing when to stop: Transcription termination on protein-coding genes by eukaryotic RNAPII.

Rodríguez-Molina, Juan B / West, Steven / Passmore, Lori A

Molecular cell

2023 Volume 83, Issue 3, Page(s) 404–415

Abstract: Gene expression is controlled in a dynamic and regulated manner to allow for the consistent and steady expression of some proteins as well as the rapidly changing production of other proteins. Transcription initiation has been a major focus of study ... ...

Abstract	Gene expression is controlled in a dynamic and regulated manner to allow for the consistent and steady expression of some proteins as well as the rapidly changing production of other proteins. Transcription initiation has been a major focus of study because it is highly regulated. However, termination of transcription also plays an important role in controlling gene expression. Transcription termination on protein-coding genes is intimately linked with 3' end cleavage and polyadenylation of transcripts, and it generally results in the production of a mature mRNA that is exported from the nucleus. Termination on many non-coding genes can also result in the production of a mature transcript. Termination is dynamically regulated-premature termination and transcription readthrough occur in response to a number of cellular signals, and these can have varied consequences on gene expression. Here, we review eukaryotic transcription termination by RNA polymerase II (RNAPII), focusing on protein-coding genes.
MeSH term(s)	RNA Polymerase II/genetics ; RNA Polymerase II/metabolism ; Transcription, Genetic ; Polyadenylation ; RNA, Messenger/genetics ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Transcription Termination, Genetic
Chemical Substances	RNA Polymerase II (EC 2.7.7.-) ; RNA, Messenger
Language	English
Publishing date	2023-01-11
Publishing country	United States
Document type	Journal Article ; Review ; Research Support, Non-U.S. Gov't ; Comment
ZDB-ID	1415236-8
ISSN	1097-4164 ; 1097-2765
ISSN (online)	1097-4164
ISSN	1097-2765
DOI	10.1016/j.molcel.2022.12.021
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Article ; Online: The long and short of it.

Passmore, Lori A / Tang, Terence Tl

eLife

2021 Volume 10

Abstract: Longer poly(A) tails improve translation in early development, but not in mature cells that have higher levels of the protein PABPC. ...

Abstract	Longer poly(A) tails improve translation in early development, but not in mature cells that have higher levels of the protein PABPC.
MeSH term(s)	Oocytes ; RNA, Messenger
Chemical Substances	RNA, Messenger
Language	English
Publishing date	2021-07-02
Publishing country	England
Document type	Editorial ; Comment
ZDB-ID	2687154-3
ISSN	2050-084X ; 2050-084X
ISSN (online)	2050-084X
ISSN	2050-084X
DOI	10.7554/eLife.70757
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Article ; Online: Roles of mRNA poly(A) tails in regulation of eukaryotic gene expression.

Passmore, Lori A / Coller, Jeff

Nature reviews. Molecular cell biology

2021 Volume 23, Issue 2, Page(s) 93–106

Abstract: In eukaryotes, poly(A) tails are present on almost every mRNA. Early experiments led to the hypothesis that poly(A) tails and the cytoplasmic polyadenylate-binding protein (PABPC) promote translation and prevent mRNA degradation, but the details remained ...

Abstract	In eukaryotes, poly(A) tails are present on almost every mRNA. Early experiments led to the hypothesis that poly(A) tails and the cytoplasmic polyadenylate-binding protein (PABPC) promote translation and prevent mRNA degradation, but the details remained unclear. More recent data suggest that the role of poly(A) tails is much more complex: poly(A)-binding protein can stimulate poly(A) tail removal (deadenylation) and the poly(A) tails of stable, highly translated mRNAs at steady state are much shorter than expected. Furthermore, the rate of translation elongation affects deadenylation. Consequently, the interplay between poly(A) tails, PABPC, translation and mRNA decay has a major role in gene regulation. In this Review, we discuss recent work that is revolutionizing our understanding of the roles of poly(A) tails in the cytoplasm. Specifically, we discuss the roles of poly(A) tails in translation and control of mRNA stability and how poly(A) tails are removed by exonucleases (deadenylases), including CCR4-NOT and PAN2-PAN3. We also discuss how deadenylation rate is determined, the integration of deadenylation with other cellular processes and the function of PABPC. We conclude with an outlook for the future of research in this field.
MeSH term(s)	Animals ; Eukaryota/genetics ; Gene Expression Regulation ; Humans ; Poly A/metabolism ; Protein Biosynthesis/genetics ; RNA Stability ; RNA, Messenger/genetics ; RNA, Messenger/metabolism
Chemical Substances	RNA, Messenger ; Poly A (24937-83-5)
Language	English
Publishing date	2021-09-30
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2031313-5
ISSN	1471-0080 ; 1471-0072
ISSN (online)	1471-0080
ISSN	1471-0072
DOI	10.1038/s41580-021-00417-y
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Zs.A 5446: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
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Article ; Online: AlphaFold: Research accelerator and hypothesis generator.

Campbell, Elizabeth A / Walden, Helen / Walter, Johannes C / Shukla, Arun K / Beck, Martin / Passmore, Lori A / Xu, H Eric

Molecular cell

2024 Volume 84, Issue 3, Page(s) 404–408

Abstract: To celebrate the 50th anniversary of Cell Press and the Cell focus issue on structural biology, we discussed with scientists working across diverse fields how AlphaFold has changed their research and brought structural biology to the masses. ...

Abstract	To celebrate the 50th anniversary of Cell Press and the Cell focus issue on structural biology, we discussed with scientists working across diverse fields how AlphaFold has changed their research and brought structural biology to the masses.
MeSH term(s)	Molecular Biology ; Anniversaries and Special Events
Language	English
Publishing date	2024-02-01
Publishing country	United States
Document type	Journal Article
ZDB-ID	1415236-8
ISSN	1097-4164 ; 1097-2765
ISSN (online)	1097-4164
ISSN	1097-2765
DOI	10.1016/j.molcel.2023.12.035
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Article ; Online: A direct interaction between CPF and RNA Pol II links RNA 3' end processing to transcription.

Carminati, Manuel / Rodríguez-Molina, Juan B / Manav, M Cemre / Bellini, Dom / Passmore, Lori A

Molecular cell

2023 Volume 83, Issue 24, Page(s) 4461–4478.e13

Abstract: Transcription termination by RNA polymerase II (RNA Pol II) is linked to RNA 3' end processing by the cleavage and polyadenylation factor (CPF or CPSF). CPF contains endonuclease, poly(A) polymerase, and protein phosphatase activities, which cleave and ... ...

Abstract	Transcription termination by RNA polymerase II (RNA Pol II) is linked to RNA 3' end processing by the cleavage and polyadenylation factor (CPF or CPSF). CPF contains endonuclease, poly(A) polymerase, and protein phosphatase activities, which cleave and polyadenylate pre-mRNAs and dephosphorylate RNA Pol II to control transcription. Exactly how the RNA 3' end processing machinery is coupled to transcription remains unclear. Here, we combine in vitro reconstitution, structural studies, and genome-wide analyses to show that yeast CPF physically and functionally interacts with RNA Pol II. Surprisingly, CPF-mediated dephosphorylation promotes the formation of an RNA Pol II stalk-to-stalk homodimer in vitro. This dimer is compatible with transcription but not with the binding of transcription elongation factors. Disruption of the dimerization interface in cells causes transcription defects, including altered RNA Pol II abundance on protein-coding genes, tRNA genes, and intergenic regions. We hypothesize that RNA Pol II dimerization may provide a mechanistic basis for the allosteric model of transcription termination.
MeSH term(s)	RNA Polymerase II/metabolism ; Saccharomyces cerevisiae Proteins/metabolism ; Genome-Wide Association Study ; Transcription, Genetic ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; RNA 3' End Processing/genetics
Chemical Substances	RNA Polymerase II (EC 2.7.7.-) ; Saccharomyces cerevisiae Proteins
Language	English
Publishing date	2023-11-28
Publishing country	United States
Document type	Journal Article
ZDB-ID	1415236-8
ISSN	1097-4164 ; 1097-2765
ISSN (online)	1097-4164
ISSN	1097-2765
DOI	10.1016/j.molcel.2023.11.004
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Article ; Online: RBBP6 activates the pre-mRNA 3' end processing machinery in humans.

Boreikaite, Vytaute / Elliott, Thomas S / Chin, Jason W / Passmore, Lori A

Genes & development

2022 Volume 36, Issue 3-4, Page(s) 210–224

Abstract: 3' end processing of most human mRNAs is carried out by the cleavage and polyadenylation specificity factor (CPSF; CPF in yeast). Endonucleolytic cleavage of the nascent pre-mRNA defines the 3' end of the mature transcript, which is important for mRNA ... ...

Abstract	3' end processing of most human mRNAs is carried out by the cleavage and polyadenylation specificity factor (CPSF; CPF in yeast). Endonucleolytic cleavage of the nascent pre-mRNA defines the 3' end of the mature transcript, which is important for mRNA localization, translation, and stability. Cleavage must therefore be tightly regulated. Here, we reconstituted specific and efficient 3' endonuclease activity of human CPSF with purified proteins. This required the seven-subunit CPSF as well as three additional protein factors: cleavage stimulatory factor (CStF), cleavage factor IIm (CFIIm), and, importantly, the multidomain protein RBBP6. Unlike its yeast homolog Mpe1, which is a stable subunit of CPF, RBBP6 does not copurify with CPSF and is recruited in an RNA-dependent manner. Sequence and mutational analyses suggest that RBBP6 interacts with the WDR33 and CPSF73 subunits of CPSF. Thus, it is likely that the role of RBBP6 is conserved from yeast to humans. Overall, our data are consistent with CPSF endonuclease activation and site-specific pre-mRNA cleavage being highly controlled to maintain fidelity in mRNA processing.
MeSH term(s)	Cleavage And Polyadenylation Specificity Factor/genetics ; Cleavage And Polyadenylation Specificity Factor/metabolism ; DNA-Binding Proteins/metabolism ; Endonucleases/metabolism ; Humans ; RNA Precursors/genetics ; RNA Precursors/metabolism ; RNA Processing, Post-Transcriptional ; RNA, Messenger/metabolism ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism ; Ubiquitin-Protein Ligases/metabolism
Chemical Substances	Cleavage And Polyadenylation Specificity Factor ; DNA-Binding Proteins ; Mpe1 protein, S cerevisiae ; RNA Precursors ; RNA, Messenger ; Saccharomyces cerevisiae Proteins ; RBBP6 protein, human (EC 2.3.2.27) ; Ubiquitin-Protein Ligases (EC 2.3.2.27) ; Endonucleases (EC 3.1.-)
Language	English
Publishing date	2022-02-17
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	806684-x
ISSN	1549-5477 ; 0890-9369
ISSN (online)	1549-5477
ISSN	0890-9369
DOI	10.1101/gad.349223.121
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Zs.MG 54: Show issues

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Article ; Online: The long and short of it

Lori A Passmore / Terence TL Tang

eLife, Vol

2021 Volume 10

Abstract: Longer poly(A) tails improve translation in early development, but not in mature cells that have higher levels of the protein PABPC. ...

Abstract	Longer poly(A) tails improve translation in early development, but not in mature cells that have higher levels of the protein PABPC.
Keywords	regulation of translation ; regulation of mRNA stability ; translation ; poly(A) tail ; PABPC1 ; Xenopus oocytes ; Medicine ; R ; Science ; Q ; Biology (General) ; QH301-705.5
Language	English
Publishing date	2021-07-01T00:00:00Z
Publisher	eLife Sciences Publications Ltd
Document type	Article ; Online
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Article ; Online: Recognition of Poly(A) RNA through Its Intrinsic Helical Structure.

Tang, Terence T L / Passmore, Lori A

Cold Spring Harbor symposia on quantitative biology

2020 Volume 84, Page(s) 21–30

Abstract: The polyadenosine (poly(A)) tail, which is found on the 3' end of almost all eukaryotic messenger RNAs (mRNAs), plays an important role in the posttranscriptional regulation of gene expression. Shortening of the poly(A) tail, a process known as ... ...

Abstract	The polyadenosine (poly(A)) tail, which is found on the 3' end of almost all eukaryotic messenger RNAs (mRNAs), plays an important role in the posttranscriptional regulation of gene expression. Shortening of the poly(A) tail, a process known as deadenylation, is thought to be the first and rate-limiting step of mRNA turnover. Deadenylation is performed by the Pan2-Pan3 and Ccr4-Not complexes that contain highly conserved exonuclease enzymes Pan2, and Ccr4 and Caf1, respectively. These complexes have been extensively studied, but the mechanisms of how the deadenylase enzymes recognize the poly(A) tail were poorly understood until recently. Here, we summarize recent work from our laboratory demonstrating that the highly conserved Pan2 exonuclease recognizes the poly(A) tail, not through adenine-specific functional groups, but through the conformation of poly(A) RNA. Our biochemical, biophysical, and structural investigations suggest that poly(A) forms an intrinsic base-stacked, single-stranded helical conformation that is recognized by Pan2, and that disruption of this structure inhibits both Pan2 and Caf1. This intrinsic structure has been shown to be important in poly(A) recognition in other biological processes, further underlining the importance of the unique conformation of poly(A).
Language	English
Publishing date	2020-04-15
Publishing country	United States
Document type	Journal Article
ISSN	1943-4456 ; 0091-7451
ISSN (online)	1943-4456
ISSN	0091-7451
DOI	10.1101/sqb.2019.84.039818
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