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Article ; Online: α-tubulin regulation by 5' introns in Saccharomyces cerevisiae.

Wethekam, Linnea C / Moore, Jeffrey K

2023 Volume 225, Issue 4

Abstract: Across eukaryotic genomes, multiple α- and β-tubulin genes require regulation to ensure sufficient production of tubulin heterodimers. Features within these gene families that regulate expression remain underexplored. Here, we investigate the role of the ...

Abstract	Across eukaryotic genomes, multiple α- and β-tubulin genes require regulation to ensure sufficient production of tubulin heterodimers. Features within these gene families that regulate expression remain underexplored. Here, we investigate the role of the 5' intron in regulating α-tubulin expression in Saccharomyces cerevisiae. We find that the intron in the α-tubulin, TUB1, promotes α-tubulin expression and cell fitness during microtubule stress. The role of the TUB1 intron depends on proximity to the TUB1 promoter and sequence features that are distinct from the intron in the alternative α-tubulin isotype, TUB3. These results lead us to perform a screen to identify genes that act with the TUB1 intron. We identified several genes involved in chromatin remodeling, α/β-tubulin heterodimer assembly, and the spindle assembly checkpoint. We propose a model where the TUB1 intron promotes expression from the chromosomal locus and that this may represent a conserved mechanism for tubulin regulation under conditions that require high levels of tubulin production.
MeSH term(s)	Tubulin/genetics ; Tubulin/metabolism ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Introns ; Microtubules/metabolism ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism
Chemical Substances	Tubulin ; Saccharomyces cerevisiae Proteins
Language	English
Publishing date	2023-08-21
Publishing country	United States
Document type	Journal Article
ZDB-ID	2167-2
ISSN	1943-2631 ; 0016-6731
ISSN (online)	1943-2631
ISSN	0016-6731
DOI	10.1093/genetics/iyad163
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Article ; Online: Tubulin isotype regulation maintains asymmetric requirement for α-tubulin over β-tubulin.

Wethekam, Linnea C / Moore, Jeffrey K

The Journal of cell biology

2023 Volume 222, Issue 3

Abstract: How cells regulate α- and β-tubulin to meet the demand for αβ-heterodimers and avoid consequences of monomer imbalance is not understood. We investigate the role of gene copy number and how shifting expression of α- or β-tubulin genes impacts tubulin ... ...

Abstract	How cells regulate α- and β-tubulin to meet the demand for αβ-heterodimers and avoid consequences of monomer imbalance is not understood. We investigate the role of gene copy number and how shifting expression of α- or β-tubulin genes impacts tubulin proteostasis and microtubule function in Saccharomyces cerevisiae. We find that α-tubulin gene copy number is important for maintaining excess α-tubulin protein compared to β-tubulin protein. Excess α-tubulin prevents accumulation of super-stoichiometric β-tubulin, which leads to loss of microtubules, formation of non-microtubule assemblies of tubulin, and disrupts cell proliferation. In contrast, sub-stoichiometric β-tubulin or overexpression of α-tubulin has minor effects. We provide evidence that yeast cells equilibrate α-tubulin protein concentration when α-tubulin isotype expression is increased. We propose an asymmetric relationship between α- and β-tubulins, in which α-tubulins are maintained in excess to supply αβ-heterodimers and limit the accumulation of β-tubulin monomers.
MeSH term(s)	Microtubules/metabolism ; Saccharomyces cerevisiae/metabolism ; Tubulin/metabolism ; Protein Isoforms/metabolism ; Gene Dosage
Chemical Substances	Tubulin ; Protein Isoforms
Language	English
Publishing date	2023-01-31
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
ZDB-ID	218154-x
ISSN	1540-8140 ; 0021-9525
ISSN (online)	1540-8140
ISSN	0021-9525
DOI	10.1083/jcb.202202102
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Article ; Online: Microtubule cytoskeleton: Revealing new readers of the tubulin code.

Wethekam, Linnea C / Moore, Jeffrey K

Current biology : CB

2022 Volume 32, Issue 18, Page(s) R960–R962

Abstract: Microtubule networks are thought to be controlled by an elaborate program of tubulin posttranslational modifications and proteins that selectively bind to modified states. A new study identifies proteins that bind tyrosinated tubulin, revealing a novel ... ...

Abstract	Microtubule networks are thought to be controlled by an elaborate program of tubulin posttranslational modifications and proteins that selectively bind to modified states. A new study identifies proteins that bind tyrosinated tubulin, revealing a novel recognition mechanism.
MeSH term(s)	Cytoskeleton/metabolism ; Microtubules/metabolism ; Protein Processing, Post-Translational ; Tubulin/metabolism
Chemical Substances	Tubulin
Language	English
Publishing date	2022-07-08
Publishing country	England
Document type	Journal Article ; Comment
ZDB-ID	1071731-6
ISSN	1879-0445 ; 0960-9822
ISSN (online)	1879-0445
ISSN	0960-9822
DOI	10.1016/j.cub.2022.08.023
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Article ; Online: Specialist α-tubulins for pluralist microtubules.

Moore, Jeffrey K / Wethekam, Linnea

The Journal of cell biology

2021 Volume 220, Issue 12

Abstract: α- and β-tubulins are encoded by multigene families, but the role of tubulin diversity for microtubule function has been a longstanding mystery. A new study (2021. J. Cell Biol.https://doi.org/10.1083/jcb.202010155) shows that the two budding yeast α- ... ...

Abstract	α- and β-tubulins are encoded by multigene families, but the role of tubulin diversity for microtubule function has been a longstanding mystery. A new study (2021. J. Cell Biol.https://doi.org/10.1083/jcb.202010155) shows that the two budding yeast α-tubulins have distinct roles during mitotic spindle positioning.
MeSH term(s)	Humans ; Microtubules ; Tubulin
Chemical Substances	Tubulin
Language	English
Publishing date	2021-11-11
Publishing country	United States
Document type	Journal Article ; Comment
ZDB-ID	218154-x
ISSN	1540-8140 ; 0021-9525
ISSN (online)	1540-8140
ISSN	0021-9525
DOI	10.1083/jcb.202110038
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Article: Quantifying yeast microtubules and spindles using the Toolkit for Automated Microtubule Tracking (TAMiT).

Ansari, Saad / Gergely, Zachary R / Flynn, Patrick / Li, Gabriella / Moore, Jeffrey K / Betterton, Meredith D

bioRxiv : the preprint server for biology

2023

Abstract: Fluorescently labeled proteins absorb and emit light, appearing as Gaussian spots in fluorescence imaging. When fluorescent tags are added to cytoskeletal polymers such as microtubules, a line of fluorescence and even non-linear structures results. While ...

Abstract	Fluorescently labeled proteins absorb and emit light, appearing as Gaussian spots in fluorescence imaging. When fluorescent tags are added to cytoskeletal polymers such as microtubules, a line of fluorescence and even non-linear structures results. While much progress has been made in techniques for imaging and microscopy, image analysis is less well developed. Current analysis of fluorescent microtubules uses either manual tools, such as kymographs, or automated software. As a result, our ability to quantify microtubule dynamics and organization from light microscopy remains limited. Despite development of automated microtubule analysis tools for
Language	English
Publishing date	2023-02-08
Publishing country	United States
Document type	Preprint
DOI	10.1101/2023.02.07.527544
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Article: The molecular biology of tubulinopathies: Understanding the impact of variants on tubulin structure and microtubule regulation.

Hoff, Katelyn J / Neumann, Andrew J / Moore, Jeffrey K

Frontiers in cellular neuroscience

2022 Volume 16, Page(s) 1023267

Abstract: Heterozygous, missense mutations in both α- and β-tubulin genes have been linked to an array of neurodevelopment disorders, commonly referred to as "tubulinopathies." To date, tubulinopathy mutations have been identified in three β-tubulin isotypes and ... ...

Abstract	Heterozygous, missense mutations in both α- and β-tubulin genes have been linked to an array of neurodevelopment disorders, commonly referred to as "tubulinopathies." To date, tubulinopathy mutations have been identified in three β-tubulin isotypes and one α-tubulin isotype. These mutations occur throughout the different genetic domains and protein structures of these tubulin isotypes, and the field is working to address how this molecular-level diversity results in different cellular and tissue-level pathologies. Studies from many groups have focused on elucidating the consequences of individual mutations; however, the field lacks comprehensive models for the molecular etiology of different types of tubulinopathies, presenting a major gap in diagnosis and treatment. This review highlights recent advances in understanding tubulin structural dynamics, the roles microtubule-associated proteins (MAPs) play in microtubule regulation, and how these are inextricably linked. We emphasize the value of investigating interactions between tubulin structures, microtubules, and MAPs to understand and predict the impact of tubulinopathy mutations at the cell and tissue levels. Microtubule regulation is multifaceted and provides a complex set of controls for generating a functional cytoskeleton at the right place and right time during neurodevelopment. Understanding how tubulinopathy mutations disrupt distinct subsets of those controls, and how that ultimately disrupts neurodevelopment, will be important for establishing mechanistic themes among tubulinopathies that may lead to insights in other neurodevelopment disorders and normal neurodevelopment.
Language	English
Publishing date	2022-11-02
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2452963-1
ISSN	1662-5102
ISSN	1662-5102
DOI	10.3389/fncel.2022.1023267
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Article ; Online: Microtubule dynamics at low temperature: evidence that tubulin recycling limits assembly.

Li, Gabriella / Moore, Jeffrey K

Molecular biology of the cell

2020 Volume 31, Issue 11, Page(s) 1154–1166

Abstract: How temperature specifically affects microtubule dynamics and how these lead to changes in microtubule networks in cells have not been established. We investigated these questions in budding yeast, an organism found in diverse environments and therefore ... ...

Abstract	How temperature specifically affects microtubule dynamics and how these lead to changes in microtubule networks in cells have not been established. We investigated these questions in budding yeast, an organism found in diverse environments and therefore predicted to exhibit dynamic microtubules across a broad temperature range. We measured the dynamics of GFP-labeled microtubules in living cells and found that lowering temperature from 37°C to 10°C decreased the rates of both polymerization and depolymerization, decreased the amount of polymer assembled before catastrophes, and decreased the frequency of microtubule emergence from nucleation sites. Lowering to 4°C caused rapid loss of almost all microtubule polymer. We provide evidence that these effects on microtubule dynamics may be explained in part by changes in the cofactor-dependent conformational dynamics of tubulin proteins. Ablation of tubulin-binding cofactors (TBCs) further sensitizes cells and their microtubules to low temperatures, and we highlight a specific role for TBCB/Alf1 in microtubule maintenance at low temperatures. Finally, we show that inhibiting the maturation cycle of tubulin by using a point mutant in β-tubulin confers hyperstable microtubules at low temperatures and rescues the requirement for TBCB/Alf1 in maintaining microtubule polymer at low temperatures. Together, these results reveal an unappreciated step in the tubulin cycle.
MeSH term(s)	Arabidopsis/metabolism ; Arabidopsis Proteins/metabolism ; Carbon-Sulfur Lyases/metabolism ; Cold Temperature ; Microtubule-Associated Proteins/metabolism ; Microtubules/metabolism ; Microtubules/physiology ; Polymerization ; Protein Binding ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/metabolism ; Temperature ; Tubulin/metabolism ; Tubulin/physiology
Chemical Substances	Arabidopsis Proteins ; Microtubule-Associated Proteins ; Saccharomyces cerevisiae Proteins ; Tubulin ; AT2G20610 protein, Arabidopsis (EC 4.4.-) ; Carbon-Sulfur Lyases (EC 4.4.-)
Language	English
Publishing date	2020-03-26
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	1098979-1
ISSN	1939-4586 ; 1059-1524
ISSN (online)	1939-4586
ISSN	1059-1524
DOI	10.1091/mbc.E19-11-0634
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Article ; Online: Nitrite Formation at a Diiron Dinitrosyl Complex.

Poptic, Anna L / Klinger, Jeffrey K / Carter, Samantha L / Moore, Curtis E / Zhang, Shiyu

Journal of the American Chemical Society

2023 Volume 145, Issue 42, Page(s) 22993–22999

Abstract: Pathogenic bacteria employ iron-containing enzymes to detoxify nitric oxide ( ... ...

Abstract	Pathogenic bacteria employ iron-containing enzymes to detoxify nitric oxide (NO
MeSH term(s)	Animals ; Nitric Oxide/chemistry ; Nitrites ; Iron/chemistry ; Oxidation-Reduction ; Nitrous Oxide ; Bacteria/metabolism ; Mammals/metabolism
Chemical Substances	Nitric Oxide (31C4KY9ESH) ; Nitrites ; Iron (E1UOL152H7) ; Nitrous Oxide (K50XQU1029)
Language	English
Publishing date	2023-10-10
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	3155-0
ISSN	1520-5126 ; 0002-7863
ISSN (online)	1520-5126
ISSN	0002-7863
DOI	10.1021/jacs.3c05155
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Article ; Online: Quantifying Yeast Microtubules and Spindles Using the Toolkit for Automated Microtubule Tracking (TAMiT).

Ansari, Saad / Gergely, Zachary R / Flynn, Patrick / Li, Gabriella / Moore, Jeffrey K / Betterton, Meredith D

Biomolecules

2023 Volume 13, Issue 6

Abstract	Fluorescently labeled proteins absorb and emit light, appearing as Gaussian spots in fluorescence imaging. When fluorescent tags are added to cytoskeletal polymers such as microtubules, a line of fluorescence and even non-linear structures results. While much progress has been made in techniques for imaging and microscopy, image analysis is less well-developed. Current analysis of fluorescent microtubules uses either manual tools, such as kymographs, or automated software. As a result, our ability to quantify microtubule dynamics and organization from light microscopy remains limited. Despite the development of automated microtubule analysis tools for in vitro studies, analysis of images from cells often depends heavily on manual analysis. One of the main reasons for this disparity is the low signal-to-noise ratio in cells, where background fluorescence is typically higher than in reconstituted systems. Here, we present the Toolkit for Automated Microtubule Tracking (TAMiT), which automatically detects, optimizes, and tracks fluorescent microtubules in living yeast cells with sub-pixel accuracy. Using basic information about microtubule organization, TAMiT detects linear and curved polymers using a geometrical scanning technique. Images are fit via an optimization problem for the microtubule image parameters that are solved using non-linear least squares in Matlab. We benchmark our software using simulated images and show that it reliably detects microtubules, even at low signal-to-noise ratios. Then, we use TAMiT to measure monopolar spindle microtubule bundle number, length, and lifetime in a large dataset that includes several
MeSH term(s)	Saccharomyces cerevisiae ; Microscopy, Fluorescence/methods ; Microtubules/metabolism ; Software
Language	English
Publishing date	2023-06-04
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	2701262-1
ISSN	2218-273X ; 2218-273X
ISSN (online)	2218-273X
ISSN	2218-273X
DOI	10.3390/biom13060939
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Article: Microbiota of maize kernels as influenced by

Moore, Geromy G / Chalivendra, Subbaiah / Mack, Brian M / Gilbert, Matthew K / Cary, Jeffrey W / Rajasekaran, Kanniah

Frontiers in microbiology

2023 Volume 14, Page(s) 1291284

Abstract: Background: Nearly everything on Earth harbors a microbiome. A microbiome is a community of microbes (bacteria, fungi, and viruses) with potential to form complex networks that involve mutualistic and antagonistic interactions. Resident microbiota on/in ...

Abstract	Background: Nearly everything on Earth harbors a microbiome. A microbiome is a community of microbes (bacteria, fungi, and viruses) with potential to form complex networks that involve mutualistic and antagonistic interactions. Resident microbiota on/in an organism are determined by the external environment, both biotic and abiotic, and the intrinsic adaptability of each organism. Although the maize microbiome has been characterized, community changes that result from the application of fungal biocontrol strains, such as non-aflatoxigenic Methods: We silk channel inoculated field-grown maize separately with a non-aflatoxigenic biocontrol strain (K49), a highly toxigenic strain (Tox4), and a combination of both Results: We found that the native microbial communities were significantly affected, irrespective of genotype or sampled tissue. Overall, bacteriomes exhibited greater diversity of genera than mycobiomes. The abundance of certain genera was unchanged by treatment, including genera of bacteria (e.g., Conclusion: Beneficial microbes like
Language	English
Publishing date	2023-11-06
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2587354-4
ISSN	1664-302X
ISSN	1664-302X
DOI	10.3389/fmicb.2023.1291284
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