Functionally non-redundant paralogs spe-47 and spe-50 encode FB-MO associated proteins and interact with him-8

The activation of C. elegans spermatids to crawling spermatozoa is affected by a number of genes including spe-47. Here, we investigate a paralog to spe-47: spe-50, which has a highly conserved sequence and expression, but which is not functionally redundant to spe-47. Phylogenetic analysis indicates that the duplication event that produced the paralogs occurred prior to the radiation of the Caenorhabditis species included in the analysis, allowing a long period for the paralogs to diverge in function. Furthermore, we observed that knockout mutations in both genes, either alone or together, have little effect on sperm function. However, hermaphrodites harboring both knockout mutations combined with a third mutation in the him-8 gene are nearly self-sterile due to a sperm defect, even though they have numerous apparently normal sperm within their spermathecae. We suggest that the sperm in these triple mutants are defective in fusing with oocytes, and that the effect of the him-8 mutation is unclear but likely due to its direct or indirect effect on local chromatin structure and function.

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Functionally non-redundant paralogs spe-47 and spe-50 encode FB-MO associated proteins and interact with him-8

10.1101/2020.03.13.990366 ◽

2020 ◽

Author(s):

Jessica N. Clark ◽

Gaurav Prajapati ◽

Fermina Aldaco ◽

Thomas J. Sokolich ◽

Steven Keung ◽

...

Keyword(s):

Phylogenetic Analysis ◽

Chromatin Remodeling ◽

Duplication Event ◽

Sperm Function ◽

C Elegans ◽

Conserved Sequence ◽

Long Period ◽

Normal Sperm ◽

Number Of Genes ◽

Associated Proteins

AbstractThe activation of C. elegans spermatids to crawling spermatozoa is affected by a number of genes including spe-47. Here, we investigate a paralog to spe-47: spe-50, which has a highly conserved sequence and expression, but which is not functionally redundant to spe-47. Phylogenetic analysis indicates that the duplication event that produced the paralogs occurred prior to the radiation of the Caenorhabditis species included in the analysis, allowing a long period for the paralogs to diverge in function. Furthermore, we observed that knockout mutations in both genes, either alone or together, have little effect on sperm function. However, hermaphrodites harboring both knockout mutations combined with a third mutation in the him-8 gene are nearly self-sterile due to a sperm defect, even though they have numerous apparently normal sperm within their spermathecae. We suggest that the sperm in these triple mutants are defective in fusing with oocytes, and that the effect of the him-8 mutation is due to its role in chromatin remodeling.

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Crystal Structures of Fragments D and Double-D from Fibrinogen and Fibrin

Thrombosis and Haemostasis ◽

10.1055/s-0037-1615842 ◽

1999 ◽

Vol 82 (08) ◽

pp. 271-276 ◽

Cited By ~ 8

Author(s):

Glen Spraggon ◽

Stephen Everse ◽

Russell Doolittle

Keyword(s):

Electron Microscopy ◽

High Resolution ◽

Crystal Structures ◽

Structure And Function ◽

X Ray ◽

Long Period ◽

And Function

IntroductionAfter a long period of anticipation,1 the last two years have witnessed the first high-resolution x-ray structures of fragments from fibrinogen and fibrin.2-7 The results confirmed many aspects of fibrinogen structure and function that had previously been inferred from electron microscopy and biochemistry and revealed some unexpected features. Several matters have remained stubbornly unsettled, however, and much more work remains to be done. Here, we review several of the most significant findings that have accompanied the new x-ray structures and discuss some of the problems of the fibrinogen-fibrin conversion that remain unresolved. * Abbreviations: GPR—Gly-Pro-Arg-derivatives; GPRPam—Gly-Pro-Arg-Pro-amide; GHRPam—Gly-His-Arg-Pro-amide

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Structure and function of seed lipid body-associated proteins

Comptes Rendus Biologies ◽

10.1016/j.crvi.2008.07.016 ◽

2008 ◽

Vol 331 (10) ◽

pp. 746-754 ◽

Cited By ~ 57

Author(s):

Zita Purkrtova ◽

Pascale Jolivet ◽

Martine Miquel ◽

Thierry Chardot

Keyword(s):

Lipid Body ◽

Structure And Function ◽

Seed Lipid ◽

Associated Proteins ◽

And Function

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Regulation of sperm motility at the axonemal level

Reproduction Fertility and Development ◽

10.1071/rd9950847 ◽

1995 ◽

Vol 7 (4) ◽

pp. 847 ◽

Cited By ~ 15

Author(s):

C Gagnon

Keyword(s):

Direct Action ◽

Mammalian Species ◽

Basic Structure ◽

Structure And Function ◽

Structural Components ◽

Long Period ◽

Different Types ◽

Radial Spokes ◽

Dynein Arms ◽

And Function

With very few exceptions, the basic structure of the 9+2 axoneme has been well preserved over a very long period of evolution from protozoa to mammais. This stability indicates that the basic structural components of the axoneme visible by electron microscopy, as well as most of the other unidentified components, have withstood the passage of time. It also means that components of the 9+2 axoneme have sufficient diversity in function to accommodate the various types of motility patterns encountered in different species of flagella. Several of the 200 polypeptides that constitute the axoneme have been identified as components of the dynein arms, radial spokes etc. but many more remain to be identified and their function(s) remain to be determined. Because this review deals with the regulation of flagellar movement at the axonemal level, it does not include regulation of flagella by extracellular factors unless these factors have a direct action on axonemal components. In this context, it is very important firstly to understand the structural components of the axoneme and how they influence and regulate axonemal movement. Different primitive organisms are mentioned in this review since major breakthroughs in our understanding of how an axoneme generates different types of movement have been made through their study. Despite some variations in structure and function of axonemal components, the basic mechanisms involved in the regulation of flagella from Chlamydomonas or sea urchin spermatozoa should also apply to the more evolved mammalian species, including human spermatozoa.

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Molecular Structure and Function of Microtubule-Associated Proteins

International Review of Cytology ◽

10.1016/s0074-7696(08)61528-4 ◽

1991 ◽

pp. 217-273 ◽

Cited By ~ 113

Author(s):

Gerhard Wiche ◽

Christian Oberkanins ◽

Adolf Himmler

Keyword(s):

Molecular Structure ◽

Structure And Function ◽

Microtubule Associated Proteins ◽

Associated Proteins ◽

And Function ◽

Molecular Structure And Function

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Identification of a 40 × 10(3) Mr centromere-associated protein in cultured mammalian cells

Journal of Cell Science ◽

10.1242/jcs.97.4.705 ◽

1990 ◽

Vol 97 (4) ◽

pp. 705-713

Author(s):

R. Balczon ◽

M.A. Accavitti ◽

B.R. Brinkley

Keyword(s):

Mammalian Cells ◽

Cell Types ◽

Immunoblot Analysis ◽

Structure And Function ◽

Interphase Nuclei ◽

Microtubule Associated Proteins ◽

Associated Proteins ◽

Cytoplasmic Microtubules ◽

And Function

Monoclonal antibodies were raised against a complex of proteins that was purified following the crosslinking of tubulin to the centromeres of CHO chromosomes using Lomant's reagent. One of the clones, hybridoma 32–9, produced antibodies that reacted with a 40 × 10(3) Mr protein present in the crosslinked complex. Furthermore, immunoblot analysis demonstrated that the 40 × 10(3) Mr antigen was present in various mammalian cell types from several different species. Indirect immunofluorescence using the antibody produced by clone 32–9 demonstrated that the 40 × 10(3) Mr antigen was associated with both spindle and cytoplasmic microtubules. In addition, centromere/kinetochore staining was detected in metaphase-arrested cells, while staining of prekinetochores in interphase nuclei was not observed. Unlike microtubule-associated proteins and microtubule-dependent ATPases, the 40 × 10(3) Mr protein did not copurify with microtubules when tubules were assembled from cellular homogenates using taxol and either GTP or GTP and AMP-PNP. Instead, the 40 × 10(3) Mr protein remained associated with the insoluble cellular material. The 40 × 10(3) Mr antigen could be released from the insoluble pelleted material by extraction with 1 M NaCl. Once solubilized, the 40 × 10(3) Mr protein was able to copurify with microtubules in assembly assays in vitro. This monoclonal antibody should serve as a valuable probe for studies of centromere/kinetochore structure and function.

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