Dictyostelium prespore-specific gene Dp87 encodes a sorus matrix protein

1994 ◽  
Vol 107 (3) ◽  
pp. 397-403 ◽  
Author(s):  
H. Nakao ◽  
A. Yamamoto ◽  
I. Takeuchi ◽  
M. Tasaka
Keyword(s):  
Matrix Protein ◽  
Specific Protein ◽  
Specific Gene ◽  
Coat Proteins ◽  
Fruiting Bodies ◽  
Protein Fragment ◽  
Microscopic Studies ◽  
Spore Coat Proteins ◽  
Space Matrix ◽  
Membranous Material

In this paper we report on the characteristics of the product of a prespore-specific gene (Dp87) of Dictyostelium discoideum. Polyclonal antibody was made against a bacterially synthesized Dp87-encoded protein fragment. Using this antibody, the product was characterized by immunochemical and immunocytological methods. It was shown that the Dp87-encoded protein is a prespore-specific protein with a molecular mass of 83 kDa, which first appears at the standing slug stage and persists in mature fruiting bodies. Western blot studies revealed the presence of an additional 81 kDa protein prior to the appearance of the 83 kDa protein from the tipped aggregate to the standing slug stage, thus indicating the former to be a precursor protein. Immunocytochemical and immunoelectron microscopic studies showed that the protein is bound to ER at the early stages of development when only the 81 kDa protein is present. At the later stages when the 83 kDa protein predominates, however, it becomes localized in prespore-specific vacuoles (PSVs) and is associated with the inner fibrous material of PSVs, but not with the peripheral membranous material. This is in contrast to spore coat proteins, which are localized in PSVs from the beginning of their appearance and associated with both structures of PSVs. In mature fruiting bodies, most Dp87 protein is localized to the interspore space (matrix) of the sori, with some left on the surface of the stalk tube. Disruptants of the Dp87 gene were also produced. Although they contained neither 81 kDa nor 83 kDa protein, they showed no phenotypic defects as compared to the parental strain.

scholarly journals Immunoelectron Microscopic Studies on Spore Coat Proteins ofBacillus megaterium

1988 ◽  
Vol 32 (10) ◽  
pp. 991-998 ◽  
Author(s):  
Masayoshi Imagawa ◽  
Mikiko Ohtsuka ◽  
Yoshihiro Nakatani ◽  
Yuichi Oku ◽  
Hussein I. El-Belbasi ◽  
...  
Keyword(s):  
Spore Coat ◽  
Coat Proteins ◽  
Microscopic Studies ◽  
Spore Coat Proteins

scholarly journals SpoVID Guides SafA to the Spore Coat inBacillus subtilis

2001 ◽  
Vol 183 (10) ◽  
pp. 3041-3049 ◽  
Author(s):  
Amanda J. Ozin ◽  
Craig S. Samford ◽  
Adriano O. Henriques ◽  
Charles P. Moran
Keyword(s):  
Direct Interaction ◽  
Spore Coat ◽  
Coat Proteins ◽  
Yeast Two Hybrid System ◽  
Spore Coat Proteins ◽  
Basement Layer ◽  
Two Hybrid ◽  
Spore Coat Protein

ABSTRACT Bacteria assemble complex structures by targeting proteins to specific subcellular locations. The protein coat that encasesBacillus subtilis spores is an example of a structure that requires coordinated targeting and assembly of more than 24 polypeptides. The earliest stages of coat assembly require the action of three morphogenetic proteins: SpoIVA, CotE, and SpoVID. In the first steps, a basement layer of SpoIVA forms around the surface of the forespore, guiding the subsequent positioning of a ring of CotE protein about 75 nm from the forespore surface. SpoVID localizes near the forespore membrane where it functions to maintain the integrity of the CotE ring and to anchor the nascent coat to the underlying spore structures. However, it is not known which spore coat proteins interact directly with SpoVID. In this study we examined the interaction between SpoVID and another spore coat protein, SafA, in vivo using the yeast two-hybrid system and in vitro. We found evidence that SpoVID and SafA directly interact and that SafA interacts with itself. Immunofluorescence microscopy showed that SafA localized around the forespore early during coat assembly and that this localization of SafA was dependent on SpoVID. Moreover, targeting of SafA to the forespore was also dependent on SpoIVA, as was targeting of SpoVID to the forespore. We suggest that the localization of SafA to the spore coat requires direct interaction with SpoVID.

Cloning and expression of a cDNA that comprises part of the gene coding for a spore coat protein of Dictyostelium discoideum

1984 ◽  
Vol 4 (11) ◽  
pp. 2273-2278
Author(s):  
B C Dowds ◽  
W F Loomis
Keyword(s):  
Dictyostelium Discoideum ◽  
Cdna Clone ◽  
Single Gene ◽  
Polyclonal Antiserum ◽  
Cloning And Expression ◽  
Spore Coat ◽  
Coat Proteins ◽  
Developmentally Regulated ◽  
Gene Coding ◽  
Spore Coat Proteins

The three major spore coat proteins of Dictyostelium discoideum are developmentally regulated, cell-type-specific proteins. They are packaged in prespore vesicles and then secreted to form the outer layer of spore coats. We have isolated a cDNA clone from the gene coding for one of these proteins, SP96, a glycoprotein of 96,000 daltons. We screened the cDNA bank by the method of hybrid select translation followed by immunoprecipitation of the translation products with SP96-specific polyclonal antiserum. We found that the gene was first transcribed into stable mRNA a few hours before the time of detection of SP96 synthesis and that the mRNA, like the protein, accumulated specifically in prespore cells and spores. SP96 constituted the same proportion of newly synthesized protein as the proportion of its message in polyadenylated RNA. SP96 appeared to be encoded by a single gene as judged by Southern blot analysis of digested genomic DNA hybridized to the cDNA clone.

scholarly journals Near Atomic Structure of an Atadenovirus Reveals a Conserved Capsid-Binding Motif and Intergenera Variations in Cementing Proteins

2020 ◽  
Author(s):  
Roberto Marabini ◽  
Gabriela N. Condezo ◽  
Josué Gómez-Blanco ◽  
Carmen San Martín
Keyword(s):  
Duplication Event ◽  
Specific Protein ◽  
Mammalian Host ◽  
Binding Motif ◽  
Coat Proteins ◽  
Human Adenoviruses ◽  
High Resolution Structure ◽  
Attachment Proteins ◽  
Protein Ix ◽  
Capsid Stability

AbstractLittle is known about the basic biology of non-human adenoviruses, which could be alternative vectors free of issues posed by preexisting immunity to human adenoviruses. We present the cryo-EM structure of a lizard atadenovirus, LAdV-2, at 3.4 Å resolution. This is the first high resolution structure of an adenovirus with non-mammalian host, and of an adenovirus not belonging to the Mastadenovirus genus. Atadenovirus capsids contain genus specific proteins LH3, p32k, and LH2, and are more thermostable than the more studied human adenoviruses. We find a large conformational difference in the internal vertex protein IIIa between mast- and atadenoviruses, induced by the presence of an extended polypeptide in the region. This polypeptide, as well as α-helical clusters located beneath the icosahedral facet, likely correspond to proteins LH2 and p32k. The external genus specific protein LH3, with a trimeric β-helix fold typical of bacteriophage host attachment proteins, contacts the hexon shell surface via a triskelion structure identical to that used by protein IX in human AdV, revealing a conserved capsid-binding motif and a possible gene duplication event. Altogether, this work shows how the network of minor coat proteins differs between AdV genera and relates to virus evolution and capsid stability properties.

Identification of proteins in the exosporium of Bacillus anthracis

Microbiology ◽  
2004 ◽  
Vol 150 (2) ◽  
pp. 355-363 ◽  
Author(s):  
Caroline Redmond ◽  
Leslie W. J. Baillie ◽  
Stephen Hibbs ◽  
Arthur J. G. Moir ◽  
Anne Moir
Keyword(s):  
Bacillus Anthracis ◽  
Amino Acid Sequences ◽  
Coat Proteins ◽  
Wild Type ◽  
Sds Page ◽  
Adsorbed Proteins ◽  
Spore Coat Proteins ◽  
Ames Strain ◽  
A Site ◽  
Novel Protein

Spores of Bacillus anthracis, the causative agent of anthrax, possess an exosporium. As the outer surface layer of these mature spores, the exosporium represents the primary contact surface between the spore and environment/host and is a site of spore antigens. The exosporium was isolated from the endospores of the B. anthracis wild-type Ames strain, from a derivative of the Ames strain cured of plasmid pXO2−, and from a previously isolated pXO1−, pXO2− doubly cured strain, B. anthracis UM23Cl2. The protein profiles of SDS-PAGE-separated exosporium extracts were similar for all three. This suggests that avirulent variants lacking either or both plasmids are realistic models for studying the exosporium from spores of B. anthracis. A number of loosely adsorbed proteins were identified from amino acid sequences determined by either nanospray-MS/MS or N-terminal sequencing. Salt and detergent washing of the exosporium fragments removed these and revealed proteins that are likely to represent structural/integral exosporium proteins. Seven proteins were identified in washed exosporium: alanine racemase, inosine hydrolase, ExsF, CotY, ExsY, CotB and a novel protein, named ExsK. CotY, ExsY and CotB are homologues of Bacillus subtilis outer spore coat proteins, but ExsF and ExsK are specific to B. anthracis and other members of the Bacillus cereus group.

scholarly journals The SPS4 gene of Saccharomyces cerevisiae encodes a major sporulation-specific mRNA.

1986 ◽  
Vol 6 (12) ◽  
pp. 4478-4485 ◽  
Author(s):  
A T Garber ◽  
J Segall
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Polyacrylamide Gel Electrophoresis ◽  
Specific Protein ◽  
Polyacrylamide Gel ◽  
In Vitro Translation ◽  
Specific Gene ◽  
Alpha Cells ◽  
Two Dimensional ◽  
Isoelectric Ph

The SPS4 gene of Saccharomyces cerevisiae, a sporulation-specific gene identified previously in a differential hybridization screen of a genomic yeast DNA library, has been characterized further. The protein encoded by this gene was inferred from its nucleotide sequence to be 38,600 daltons with an isoelectric pH of 8.2. Consistent with this, two-dimensional polyacrylamide gel electrophoresis of the in vitro translation products of RNA purified by hybridization with the cloned SPS4 DNA indicated that the SPS4 gene product is a 39-kilodalton, basic protein. This protein was found to be identical in size and charge to a major, sporulation-specific protein identified in a two-dimensional polyacrylamide gel electrophoretic comparison of the in vitro translation products of total RNA from sporulating MATa/MAT alpha cells and asporogenous MAT alpha/MAT alpha cells. A MATa/MAT alpha strain homozygous for a partial deletion of the SPS4 gene appeared, however, to be unaffected in its ability to form viable ascospores.

Identification of a novel kidney-specific gene downregulated in acute ischemic renal failure

2000 ◽  
Vol 279 (3) ◽  
pp. F426-F439 ◽  
Author(s):  
Erding Hu ◽  
Zunxuan Chen ◽  
Todd Fredrickson ◽  
Miklos Gellai ◽  
Malcolm Jugus ◽  
...  
Keyword(s):  
Renal Failure ◽  
Renal Function ◽  
Molecular Mechanisms ◽  
Specific Protein ◽  
Kidney Cortex ◽  
Specific Gene ◽  
Mrna Levels ◽  
Ischemic Renal Failure ◽  
New Gene

To gain further insights into the molecular mechanisms involved in acute renal failure, we have isolated a new gene from rat and human, named KSP32 (kidney-specific protein with a molecular mass of 32 kDa). KSP32 encodes a novel gene that shows little homology to other mammalian proteins. It, however, shares extensive homology with several proteins found in the nematode Caenorhabditis elegans and plants. The expression of KSP32 mRNA is highly restricted to kidney. In situ hybidization analysis revealed that the expression of KSP32 mRNA was prominent in the boundary of kidney cortex and outer medulla, exhibiting a raylike formation extending from the medulla into the cortex. Finally, KSP32 mRNA was dramatically downregulated in rat following induction of acute ischemic renal failure. Rapid loss of KSP32 mRNA expression was observed beginning at ∼5 h following renal injury and mRNA levels remained depressed for at least 96 h. Both KSP32 mRNA levels as well as renal function recovered 14 days after injury. Administration of an endothelin receptor antagonist (SB-209670), known to restore renal function, significantly increased KSP32 expression.

scholarly journals Synthesis and Deposition of Spore Coat Proteins during Sporulation ofBacillus megaterium

1985 ◽  
Vol 29 (12) ◽  
pp. 1151-1162 ◽  
Author(s):  
Masayoshi Imagawa ◽  
Yuichi Oku ◽  
Hussein I. El-Belbasi ◽  
Mie Teraoka ◽  
Tsutomu Nishihara ◽  
...  
Keyword(s):  
Spore Coat ◽  
Coat Proteins ◽  
Spore Coat Proteins
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