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Article: Fly-CURE, a multi-institutional CURE using

Merkle, Julie A / Devergne, Olivier / Kelly, Seth M / Croonquist, Paula A / Evans, Cory J / Hwalek, Melanie A / Straub, Victoria L / Hamill, Danielle R / Peister, Alexandra / Puthoff, David P / Saville, Ken J / Siders, Jamie L / Villanueva Gonzalez, Zully J / Wittke-Thompson, Jacqueline K / Bieser, Kayla L / Stamm, Joyce / Vrailas-Mortimer, Alysia D / Kagey, Jacob D

Journal of microbiology & biology education

2023 Volume 24, Issue 3

Abstract: The Fly-CURE is a genetics-focused multi-institutional Course-Based Undergraduate Research Experience (CURE) that provides undergraduate students with hands-on research experiences within a course. Through the Fly-CURE, undergraduate students at diverse ... ...

Abstract	The Fly-CURE is a genetics-focused multi-institutional Course-Based Undergraduate Research Experience (CURE) that provides undergraduate students with hands-on research experiences within a course. Through the Fly-CURE, undergraduate students at diverse types of higher education institutions across the United States map and characterize novel mutants isolated from a genetic screen in
Language	English
Publishing date	2023-09-21
Publishing country	United States
Document type	Journal Article
ISSN	1935-7877
ISSN	1935-7877
DOI	10.1128/jmbe.00245-22
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Article: Fly-CURE, a Multi-institutional CURE using

Merkle, Julie A / Devergne, Olivier / Kelly, Seth M / Croonquist, Paula A / Evans, Cory J / Hwalek, Melanie A / Straub, Victoria L / Hamill, Danielle R / Puthoff, David P / Saville, Kenneth J / Siders, Jamie L / Gonzalez, Zully J Villanueva / Wittke-Thompson, Jackie K / Bieser, Kayla L / Stamm, Joyce / Vrailas-Mortimer, Alysia D / Kagey, Jacob D

bioRxiv : the preprint server for biology

2023

Abstract	The Fly-CURE is a genetics-focused multi-institutional Course-Based Undergraduate Research Experience (CURE) that provides undergraduate students with hands-on research experiences within a course. Through the Fly-CURE, undergraduate students at diverse types of higher education institutions across the United States map and characterize novel mutants isolated from a genetic screen in
Language	English
Publishing date	2023-01-19
Publishing country	United States
Document type	Preprint
DOI	10.1101/2023.01.16.524319
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Article ; Online: Centriolar SAS-7 acts upstream of SPD-2 to regulate centriole assembly and pericentriolar material formation.

Sugioka, Kenji / Hamill, Danielle R / Lowry, Joshua B / McNeely, Marie E / Enrick, Molly / Richter, Alyssa C / Kiebler, Lauren E / Priess, James R / Bowerman, Bruce

eLife

2017 Volume 6

Abstract: The centriole/basal body is a eukaryotic organelle that plays essential roles in cell division and signaling. Among five known core centriole proteins, SPD-2/Cep192 is the first recruited to the site of daughter centriole formation and regulates the ... ...

Abstract	The centriole/basal body is a eukaryotic organelle that plays essential roles in cell division and signaling. Among five known core centriole proteins, SPD-2/Cep192 is the first recruited to the site of daughter centriole formation and regulates the centriolar localization of the other components in
MeSH term(s)	Animals ; Caenorhabditis elegans/genetics ; Caenorhabditis elegans/physiology ; Caenorhabditis elegans Proteins/metabolism ; Cell Cycle Proteins/metabolism ; Centrioles/metabolism ; Humans ; Organelle Biogenesis
Chemical Substances	Caenorhabditis elegans Proteins ; Cell Cycle Proteins ; SAS-6 protein, C elegans ; SPD-2 protein, C elegans
Language	English
Publishing date	2017-01-16
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
ZDB-ID	2687154-3
ISSN	2050-084X ; 2050-084X
ISSN (online)	2050-084X
ISSN	2050-084X
DOI	10.7554/eLife.20353
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Article: Centrosome maturation and mitotic spindle assembly in C. elegans require SPD-5, a protein with multiple coiled-coil domains.

Hamill, Danielle R / Severson, Aaron F / Carter, J Clayton / Bowerman, Bruce

Developmental cell

2002 Volume 3, Issue 5, Page(s) 673–684

Abstract: The maternally expressed C. elegans gene spd-5 encodes a centrosomal protein with multiple coiled-coil domains. During mitosis in mutants with reduced levels of SPD-5, microtubules assemble but radiate from condensed chromosomes without forming a spindle, ...

Abstract	The maternally expressed C. elegans gene spd-5 encodes a centrosomal protein with multiple coiled-coil domains. During mitosis in mutants with reduced levels of SPD-5, microtubules assemble but radiate from condensed chromosomes without forming a spindle, and mitosis fails. SPD-5 is required for the centrosomal localization of gamma-tubulin, XMAP-215, and Aurora A kinase family members, but SPD-5 accumulates at centrosomes in mutants lacking these proteins. Furthermore, SPD-5 interacts genetically with a dynein heavy chain. We propose that SPD-5, along with dynein, is required for centrosome maturation and mitotic spindle assembly.
MeSH term(s)	Amino Acid Sequence ; Animals ; Caenorhabditis elegans/embryology ; Caenorhabditis elegans/genetics ; Caenorhabditis elegans/metabolism ; Caenorhabditis elegans Proteins/genetics ; Caenorhabditis elegans Proteins/metabolism ; Centrosome/metabolism ; Centrosome/physiology ; Dyneins/metabolism ; Female ; Gene Expression ; Male ; Meiosis/physiology ; Microtubule-Associated Proteins/genetics ; Microtubule-Associated Proteins/metabolism ; Microtubules/metabolism ; Microtubules/physiology ; Molecular Sequence Data ; Mutagenesis ; Protein Structure, Tertiary ; Spindle Apparatus/physiology
Chemical Substances	Caenorhabditis elegans Proteins ; Microtubule-Associated Proteins ; Dyneins (EC 3.6.4.2)
Language	English
Publishing date	2002-11-13
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	2054967-2
ISSN	1878-1551 ; 1534-5807
ISSN (online)	1878-1551
ISSN	1534-5807
DOI	10.1016/s1534-5807(02)00327-1
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Article: Seawi--a sea urchin piwi/argonaute family member is a component of MT-RNP complexes.

Rodriguez, Alexis J / Seipel, Susan A / Hamill, Danielle R / Romancino, Daniele P / DI Carlo, Marta / Suprenant, Kathy A / Bonder, Edward M

RNA (New York, N.Y.)

2003 Volume 11, Issue 5, Page(s) 646–656

Abstract: The piwi/argonaute family of proteins is involved in key developmental processes such as stem cell maintenance and axis specification through molecular mechanisms that may involve RNA silencing. Here we report on the cloning and characterization of the ... ...

Abstract	The piwi/argonaute family of proteins is involved in key developmental processes such as stem cell maintenance and axis specification through molecular mechanisms that may involve RNA silencing. Here we report on the cloning and characterization of the sea urchin piwi/argonaute family member seawi. Seawi is a major component of microtubule-ribonucleoprotein (MT-RNP) complexes isolated from two different species of sea urchin, Strongylocentrotus purpuratus and Paracentrotus lividus. Seawi co-isolates with purified ribosomes, cosediments with 80S ribosomes in sucrose density gradients, and binds microtubules. Seawi possesses the RNA binding motif common to piwi family members and binds P. lividus bep4 mRNA, a transcript that co-isolates with MT-RNP complexes and whose translation product has been shown to play a role in patterning the animal-vegetal axis. Indirect immunofluorescence studies localized seawi to the cortex of unfertilized eggs within granule-like particles, the mitotic spindle during cell division, and the small micromeres where its levels were enriched during the early cleavage stage. Lastly, we discuss how seawi, as a piwi/argonaute family member, may play a fundamentally important role in sea urchin animal-vegetal axis formation and stem cell maintenance.
MeSH term(s)	Amino Acid Sequence ; Animals ; Cloning, Molecular ; Gene Expression Regulation, Developmental ; Gene Library ; Membrane Proteins/genetics ; Microtubules/chemistry ; Microtubules/metabolism ; Molecular Sequence Data ; Molecular Weight ; Multiprotein Complexes/chemistry ; Multiprotein Complexes/metabolism ; Protein Binding ; Proteins/chemistry ; Proteins/classification ; Proteins/genetics ; Proteins/metabolism ; RNA, Messenger/genetics ; RNA, Messenger/metabolism ; Ribonucleoproteins/chemistry ; Ribonucleoproteins/metabolism ; Ribosomes/metabolism ; Sea Urchins/classification ; Sea Urchins/embryology ; Sea Urchins/genetics ; Sequence Analysis, DNA
Chemical Substances	Bep4 protein, Paracentrotus lividus ; Membrane Proteins ; Multiprotein Complexes ; Proteins ; RNA, Messenger ; Ribonucleoproteins
Language	English
Publishing date	2003-01-10
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	1241540-6
ISSN	1355-8382
ISSN	1355-8382
DOI	10.1261/rna.7198205
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Zs.A 4777: Show issues

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Article ; Online: Genetic Mapping of a new

Siders, Jamie L / Bieser, Kayla L / Hamill, Danielle R / Acosta, Erika C / Alexander, Olivia K / Ali, Humza I / Anderson, Micah J / Arrasmith, Hayden R / Azam, Mustafa / Beeman, Nikki J / Beydoun, Hassan / Bishop, Lauren J / Blair, Morgan D / Bletch, Brianna / Bline, Heather R / Brown, Jennifer C / Burns, Kelly M / Calagua, Karina C / Chafin, Lexie /

Christy, William Ah / Ciamacco, Carlyn / Cizauskas, Hannah / Colwell, Caitlyn M / Courtright, Abigail R / Diaz Alavez, Lucero / Ecret, Rayne Is / Edriss, Fatima / Ellerbrock, Taylor G / Ellis, Madison M / Extine, Erica M / Feldman, Eric / Fickenworth, Luke J / Goeller, Caroline M / Grogg, Alexis S / Hernandez, Yailine / Hershner, Abigail / Jauss, Megan M / Jimenez Garcia, Leyre / Franks, Katey E / Kazubski, Ethan T / Landis, Emily R / Langub, Jon / Lassek, Tia N / Le, Triet C / Lee, Julia M / Levine, Daniel P / Lightfoot, Phoebe J / Love, Natasha / Maalhagh-Fard, Ali / Maguire, Colin / McGinnis, Brynna E / Mehta, Bhargavi V / Melendrez, Veronica / Mena, Zimri E / Mendell, Seth / Montiel-Garcia, Petra / Murry, Autumn S / Newland, Riley A / Nobles, Ryan M / Patel, Neha / Patil, Yashodhara / Pfister, Cassidy L / Ramage, Victoria / Ray, Mya R / Rodrigues, Joseph / Rodriquez, Victoria C / Romero, Yara / Scott, Alexandra M / Shaba, Nicholas / Sieg, Samantha / Silva, Kayla / Singh, Sahiba / Spargo, Aleksandria J / Spitnale, Savanna J / Sweeden, Nicole / Tague, Logan / Tavernini, Breanna M / Tran, Kathleen / Tungol, Liselle / Vestal, Kylie A / Wetherbee, Amber / Wright, Kayla M / Yeager, Anthony T / Zahid, Rehab / Kagey, Jacob D

microPublication biology

2021 Volume 2021

Abstract: Genetic screens provide a mechanism to identify genes involved with different cellular and organismal processes. Using a Flp/FRT screen in ... ...

Abstract	Genetic screens provide a mechanism to identify genes involved with different cellular and organismal processes. Using a Flp/FRT screen in the
Language	English
Publishing date	2021-04-08
Publishing country	United States
Document type	Journal Article
ISSN	2578-9430
ISSN (online)	2578-9430
DOI	10.17912/micropub.biology.000383
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Article ; Online: Cytoskeletal regulation by the Nedd8 ubiquitin-like protein modification pathway.

Kurz, Thimo / Pintard, Lionel / Willis, John H / Hamill, Danielle R / Gönczy, Pierre / Peter, Matthias / Bowerman, Bruce

Science (New York, N.Y.)

2002 Volume 295, Issue 5558, Page(s) 1294–1298

Abstract: The Nedd8 ubiquitin-like protein modification pathway regulates cell-cycle progression. Our analysis of Nedd8 requirements during Caenorhabditis elegans embryogenesis indicates that the cytoskeleton is another target. Nedd8 conjugation negatively ... ...

Abstract	The Nedd8 ubiquitin-like protein modification pathway regulates cell-cycle progression. Our analysis of Nedd8 requirements during Caenorhabditis elegans embryogenesis indicates that the cytoskeleton is another target. Nedd8 conjugation negatively regulated contractility of the microfilament-rich cell cortex during pronuclear migration and again during cytokinesis. The Nedd8 pathway also was required after meiosis to negatively regulate katanin, a microtubule-severing complex, permitting the assembly of a large mitotic spindle. We propose that Nedd8-modified cullin, as part of an E3 ubiquitin ligase complex, targets katanin for degradation during the transition from meiosis to mitosis.
MeSH term(s)	Actin Cytoskeleton/physiology ; Actin Cytoskeleton/ultrastructure ; Adenosine Triphosphatases/genetics ; Adenosine Triphosphatases/metabolism ; Animals ; Caenorhabditis elegans/embryology ; Caenorhabditis elegans/genetics ; Caenorhabditis elegans/metabolism ; Caenorhabditis elegans Proteins/genetics ; Caenorhabditis elegans Proteins/metabolism ; Cell Cycle Proteins/genetics ; Cell Cycle Proteins/metabolism ; Cell Division ; Cell Membrane/ultrastructure ; Cell Nucleus/physiology ; Cell Nucleus/ultrastructure ; Cullin Proteins ; Embryo, Nonmammalian/metabolism ; Genes, Helminth ; Katanin ; Meiosis ; Microtubules/drug effects ; Microtubules/physiology ; Microtubules/ultrastructure ; Mitosis ; Mutation ; Nocodazole/pharmacology ; RNA, Helminth/genetics ; Spindle Apparatus/physiology ; Spindle Apparatus/ultrastructure ; Ubiquitins/genetics ; Ubiquitins/metabolism
Chemical Substances	CUL2 protein, human ; CUL3 protein, human ; Caenorhabditis elegans Proteins ; Cell Cycle Proteins ; Cullin Proteins ; RNA, Helminth ; Ubiquitins ; Adenosine Triphosphatases (EC 3.6.1.-) ; MEI-1 protein, C elegans (EC 3.6.1.-) ; Katanin (EC 3.6.4.3) ; Nocodazole (SH1WY3R615)
Language	English
Publishing date	2002-02-15
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	128410-1
ISSN	1095-9203 ; 0036-8075
ISSN (online)	1095-9203
ISSN	0036-8075
DOI	10.1126/science.1067765
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Zs.A 27: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
Zs.MG 77: Show issues

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Article ; Online: Genetic mapping of

Mast, Elizabeth / Bieser, Kayla L / Abraham-Villa, Mary / Adams, Vanessa / Akinlehin, Akinwonuola J / Aquino, Lynarose Z / Austin, Joseph L / Austin, Abigail K / Beckham, Carissa N / Bengson, Ethan J / Bieszk, Amanda / Bogard, Brianna L / Brennan, Rowan C / Brnot, Rebecca M / Cirone, Nicholas J / Clark, Mason R / Cooper, Brianna N / Cruz, Dennys / Daprizio, Katlyn A /

DeBoe, Jason / Dencker, Michaela M / Donnelly, Laura L / Driscoll, Leanne / DuBeau, Ryan J / Durso, Sirada W / Ejub, Adam / Elgosbi, Waad / Estrada, Melanie / Evins, Kaeli / Fox, Pearl D / France, Jacob M / Franco Hernandez, Maira G / Garcia, Lizbeth A / Garl, Olivia / Gorsuch, Myeerah R / Gorzeman-Mohr, Mikayla A / Grothouse, Madison E / Gubbels, Megan E / Hakemiamjad, Romina / Harvey, Chloé V / Hoeppner, Madeline A / Ivanov, Jessica L / Johnson, Veronica M / Johnson, Jessica L / Johnson, Ashton / Johnston, Kaleigh / Keller, Katie R / Kennedy, Breanna T / Killian, Levi R / Klumb, Marissa / Koehn, Olivia L / Koym, Aaron S / Kress, Kari J / Landis, Regan E / Lewis, Kaitlyn N / Lim, Enosh / Lopez, Ilcen K / Lowe, D'Artagnan / Luengo Carretero, Paula / Lunaburg, Grace / Mallinder, Samantha L / Marshall, Natalie A / Mathew, Jessica / Mathew, Jasmine / Mcmanaway, Hailee S / Meegan, Emily N / Meyst, Jacob D / Miller, Meredith J / Minogue, Colin K / Mohr, Alina A / Moran, Cristhian I / Moran, Adrian / Morris, Morgan D / Morrison, Michael D / Moses, Emmily A / Mullins, Cade J / Neri, Citlalli I / Nichols, Jess M / Nickels, Breanna R / Okai, Akosua M / Okonmah, Chiedu / Paramo, Makena / Paramo, Meagan / Parker, Sydney L / Parmar, Neil K / Paschal, Jacob / Patel, Prem / Patel, Deep / Perkins, Erica B / Perry, Madelyn M / Perry, Zachary / Pollock, Amanda A / Portalatin, Oxxyris / Proffitt, Kamron S / Queen, Jason T / Quemeneur, Alexis C / Richardson, Amelia G / Rosenberger, Kaylee / Rutherford, Allison M / Santos-Perez, Itchel X / Sarti, Christy Y / Schouweiler, Lacey J / Sessing, Lauren M / Setaro, Sara O / Silvestri, Christopher F / Smith, Olivia A / Smith, Mackenzie J / Sumner, Jayson C / Sutton, Rachel R / Sweckard, Lindsay / Talbott, Nicholas B / Traxler, Peyton A / Truesdell, Jenna / Valenti, Aaron F / Verace, Leif / Vijayakumar, Pragathi / Wadley, William L / Walter, Katherine E / Williams, Ayanna R / Wilson, Trey J / Witbeck, Makayla A / Wobler, Trinity M / Wright, Lucas J / Zuczkowska, Karolina A / Devergne, Olivier / Hamill, Danielle R / Shah, Hemin P / Siders, Jamie / Taylor, Elizabeth E / Vrailas-Mortimer, Alysia D / Kagey, Jacob D

microPublication biology

2022 Volume 2022

Language	English
Publishing date	2022-03-18
Publishing country	United States
Document type	Journal Article
ISSN	2578-9430
ISSN (online)	2578-9430
DOI	10.17912/micropub.biology.000542
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Article ; Online: A survey of new temperature-sensitive, embryonic-lethal mutations in C. elegans: 24 alleles of thirteen genes.

PloS one

2011 Volume 6, Issue 3, Page(s) e16644

Abstract: To study essential maternal gene requirements in the early C. elegans embryo, we have screened for temperature-sensitive, embryonic lethal mutations in an effort to bypass essential zygotic requirements for such genes during larval and adult germline ... ...

Abstract	To study essential maternal gene requirements in the early C. elegans embryo, we have screened for temperature-sensitive, embryonic lethal mutations in an effort to bypass essential zygotic requirements for such genes during larval and adult germline development. With conditional alleles, multiple essential requirements can be examined by shifting at different times from the permissive temperature of 15°C to the restrictive temperature of 26°C. Here we describe 24 conditional mutations that affect 13 different loci and report the identity of the gene mutations responsible for the conditional lethality in 22 of the mutants. All but four are mis-sense mutations, with two mutations affecting splice sites, another creating an in-frame deletion, and one creating a premature stop codon. Almost all of the mis-sense mutations affect residues conserved in orthologs, and thus may be useful for engineering conditional mutations in other organisms. We find that 62% of the mutants display additional phenotypes when shifted to the restrictive temperature as L1 larvae, in addition to causing embryonic lethality after L4 upshifts. Remarkably, we also found that 13 out of the 24 mutations appear to be fast-acting, making them particularly useful for careful dissection of multiple essential requirements. Our findings highlight the value of C. elegans for identifying useful temperature-sensitive mutations in essential genes, and provide new insights into the requirements for some of the affected loci.
MeSH term(s)	Alleles ; Amino Acid Sequence ; Animals ; Caenorhabditis elegans/embryology ; Caenorhabditis elegans/enzymology ; Caenorhabditis elegans/genetics ; Caenorhabditis elegans Proteins/chemistry ; Caenorhabditis elegans Proteins/genetics ; Embryo, Nonmammalian/metabolism ; Embryo, Nonmammalian/pathology ; Genes, Helminth/genetics ; Genes, Lethal/genetics ; Larva/genetics ; Molecular Sequence Data ; Mutation/genetics ; Phenotype ; Sequence Analysis, DNA ; Temperature
Chemical Substances	Caenorhabditis elegans Proteins
Language	English
Publishing date	2011-03-01
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2267670-3
ISSN	1932-6203 ; 1932-6203
ISSN (online)	1932-6203
ISSN	1932-6203
DOI	10.1371/journal.pone.0016644
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