scholarly journals Maybe repressed mRNAs are not stored in the chromatoid body in mammalian spermatids

Reproduction ◽  
2011 ◽  
Vol 142 (3) ◽  
pp. 383-388 ◽  
Author(s):  
Kenneth C Kleene ◽  
Danielle L Cullinane
Keyword(s):  
Caenorhabditis Elegans ◽  
Mrna Translation ◽  
Mrna Localization ◽  
Structure And Function ◽  
Convincing Evidence ◽  
Chromatoid Body ◽  
P Granules ◽  
Accurate Indication ◽  
And Function ◽  
Translational Apparatus

The chromatoid body is a dynamic organelle that is thought to coordinate the cytoplasmic regulation of mRNA translation and degradation in mammalian spermatids. The chromatoid body is also postulated to function in repression of mRNA translation by sequestering dormant mRNAs where they are inaccessible to the translational apparatus. This review finds no convincing evidence that dormant mRNAs are localized exclusively in the chromatoid body. This discrepancy can be explained by two hypotheses. First, experimental artifacts, possibly related to peculiarities of the structure and function of the chromatoid body, preclude obtaining an accurate indication of mRNA localization. Second, mRNA is not stored in the chromatoid body, because, like perinuclear P granules in Caenorhabditis elegans, the chromatoid body functions as a center for mRNP remodeling and export to other cytoplasmic sites.

Age-related changes of mitochondrial structure and function in Caenorhabditis elegans

2006 ◽  
Vol 127 (10) ◽  
pp. 763-770 ◽  
Author(s):  
Kayo Yasuda ◽  
Takamasa Ishii ◽  
Hitoshi Suda ◽  
Akira Akatsuka ◽  
Philip S. Hartman ◽  
...  
Keyword(s):  
Caenorhabditis Elegans ◽  
Structure And Function ◽  
Mitochondrial Structure ◽  
Age Related ◽  
And Function ◽  
Age Related Changes

scholarly journals CHE-3, a Cytosolic Dynein Heavy Chain, Is Required for Sensory Cilia Structure and Function in Caenorhabditis elegans

2000 ◽  
Vol 221 (2) ◽  
pp. 295-307 ◽  
Author(s):  
Stephen R. Wicks ◽  
Corry J. de Vries ◽  
Henri G.A.M. van Luenen ◽  
Ronald H.A. Plasterk
Keyword(s):  
Caenorhabditis Elegans ◽  
Heavy Chain ◽  
Structure And Function ◽  
Dynein Heavy Chain ◽  
Sensory Cilia ◽  
And Function

scholarly journals Him-10 Is Required for Kinetochore Structure and Function on Caenorhabditis elegans Holocentric Chromosomes

2001 ◽  
Vol 153 (6) ◽  
pp. 1227-1238 ◽  
Author(s):  
Mary Howe ◽  
Kent L. McDonald ◽  
Donna G. Albertson ◽  
Barbara J. Meyer
Keyword(s):  
Caenorhabditis Elegans ◽  
Structure And Function ◽  
Holocentric Chromosomes ◽  
Molecular Architecture ◽  
Mitotic Chromosomes ◽  
C Elegans ◽  
Meiotic Chromosomes ◽  
Evolutionarily Conserved ◽  
And Function ◽  
Chromosome Nondisjunction

Macromolecular structures called kinetochores attach and move chromosomes within the spindle during chromosome segregation. Using electron microscopy, we identified a structure on the holocentric mitotic and meiotic chromosomes of Caenorhabditis elegans that resembles the mammalian kinetochore. This structure faces the poles on mitotic chromosomes but encircles meiotic chromosomes. Worm kinetochores require the evolutionarily conserved HIM-10 protein for their structure and function. HIM-10 localizes to the kinetochores and mediates attachment of chromosomes to the spindle. Depletion of HIM-10 disrupts kinetochore structure, causes a failure of bipolar spindle attachment, and results in chromosome nondisjunction. HIM-10 is related to the Nuf2 kinetochore proteins conserved from yeast to humans. Thus, the extended kinetochores characteristic of C. elegans holocentric chromosomes provide a guide to the structure, molecular architecture, and function of conventional kinetochores.

Opioids

2010 ◽  
pp. 125-136
Author(s):  
Michael I. Bennett
Keyword(s):  
Neuropathic Pain ◽  
Opioid Receptor ◽  
Analgesic Efficacy ◽  
Structure And Function ◽  
Convincing Evidence ◽  
Substantial Evidence ◽  
Receptor Structure ◽  
And Function

Opioid receptor structure and function can be altered in neuropathic pain states, leading to reduced sensitivity to opioids Opioids were thought to be ineffective for neuropathic pain but substantial evidence exists to demonstrate analgesic efficacy, in some cases superior to more commonly used co-analgesics The most convincing evidence supports use of morphine, oxycodone, and tramadol in neuropathic pain...

scholarly journals Cellular roles of the human Obg-like ATPase 1 (hOLA1) and its YchF homologs

2020 ◽  
Vol 98 (1) ◽  
pp. 1-11 ◽  
Author(s):  
Nirujah Balasingam ◽  
Harland E. Brandon ◽  
Joseph A. Ross ◽  
Hans-Joachim Wieden ◽  
Nehal Thakor
Keyword(s):  
Stress Response ◽  
Mammalian Cells ◽  
Binding Proteins ◽  
Mrna Translation ◽  
Nucleotide Binding ◽  
Structure And Function ◽  
Cellular Stress Response ◽  
Related Family ◽  
And Function ◽  
Nucleotide Binding Proteins

P-loop NTPases comprise one of the major superfamilies of nucleotide binding proteins, which mediate a variety of cellular processes, such as mRNA translation, signal transduction, cell motility, and growth regulation. In this review, we discuss the structure and function of two members of the ancient Obg-related family of P-loop GTPases: human Obg-like ATPase 1 (hOLA1), and its bacterial/plant homolog, YchF. After a brief discussion of nucleotide binding proteins in general and the classification of the Obg-related family in particular, we discuss the sequence and structural features of YchF and hOLA1. We then explore the various functional roles of hOLA1 in mammalian cells during stress response and cancer progression, and of YchF in bacterial cells. Finally, we directly compare and contrast the structure and function of hOLA1 with YchF before summarizing the future perspectives of hOLA1 research. This review is timely, given the variety of recent studies aimed at understanding the roles of hOLA1 and YchF in such critical processes as cellular-stress response, oncogenesis, and protein synthesis.

scholarly journals A VISIBLE ALLELE OF THE MUSCLE GENE sup-10 X OF C. ELEGANS

Genetics ◽  
1986 ◽  
Vol 113 (1) ◽  
pp. 63-72
Author(s):  
Iva Greenwald ◽  
H Robert Horvitz
Keyword(s):  
Caenorhabditis Elegans ◽  
Protein Complex ◽  
Structure And Function ◽  
The Other ◽  
Wild Type ◽  
C Elegans ◽  
Muscle Structure ◽  
New Gene ◽  
Muscle Gene ◽  
And Function

ABSTRACT In this paper, we extend our previous analyses of a set of genes in Caenorhabditis elegans that are involved in muscle structure and function: unc-93 III, sup-9 II, sup-10 X and sup-11 I. We describe an unusual, visible allele of sup-10, examine how this allele interacts genetically with mutations in other genes of this set and propose that the wild-type products of the unc-93 and sup-10 loci may be components of a protein complex. We also describe a new gene of this set, sup-18 III, and the interaction of sup-18 alleles with mutations in the other genes.

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