Isolation, sequence analysis and characterization of cDNA clones coding for the C chain of mouse C1q. Sequence similarity of complement subcomponent C1q, collagen type VIII and type X and precerebellin

Molecular cloning and complete nucleotide sequencing of Penicillium chrysogenum virus (PcV) dsRNAs indicated that PcV virions contained four dsRNA segments with sizes of 3562, 3200, 2976 and 2902 bp. Each dsRNA segment had unique sequences and contained a single large open reading frame (ORF). In vitro translation of transcripts derived from full-length cDNA clones of PcV dsRNAs yielded single products of sizes similar to those predicted from the deduced amino acid sequences of the individual ORFs. Sequence similarity searches revealed that dsRNA1 encodes a putative RNA-dependent RNA polymerase. In this study, it was determined that dsRNA2 encodes the major capsid protein and that p4, encoded by dsRNA4, is virion-associated as a minor component. All four dsRNAs of PcV, like the genomic segments of viruses with multipartite genomes, were found to have extended regions of highly conserved terminal sequences at both ends. In addition to the strictly conserved 5′-terminal 10 nt, a second region consisting of reiteration of the sequence CAA was found immediately upstream of the AUG initiator codon. These (CAA) n repeats are reminiscent of the translational enhancer elements of tobamoviruses. The 3′-terminal 14 nt were also strictly conserved. As PcV and related viruses with four dsRNA segments (genus Chrysovirus) have not been previously characterized at the molecular level, they were provisionally classified in the family Partitiviridae, comprising viruses with bipartite genomes. This study represents the first report on molecular characterization of a chrysovirus and the results suggest the creation of a new family of mycoviruses with multipartite dsRNA genomes to accommodate PcV and related viruses.

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Nuclear-encoded chloroplast ribosomal protein L12 of Nicotians tabacum: characterization of mature protein and isolation and sequence analysis of cDNA clones encoding its cytoplasmic precursor

Nucleic Acids Research ◽

10.1093/nar/20.4.689 ◽

1992 ◽

Vol 20 (4) ◽

pp. 689-697 ◽

Cited By ~ 10

Author(s):

Gasmalla A. EIhag ◽

Frank J. Thomas ◽

Thomas P. McCreery ◽

Don P. Bourque

Keyword(s):

Sequence Analysis ◽

Ribosomal Protein ◽

Cdna Clones ◽

Mature Protein

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Radixin is a novel member of the band 4.1 family.

The Journal of Cell Biology ◽

10.1083/jcb.115.4.1039 ◽

1991 ◽

Vol 115 (4) ◽

pp. 1039-1048 ◽

Cited By ~ 94

Author(s):

N Funayama ◽

A Nagafuchi ◽

N Sato ◽

S Tsukita ◽

S Tsukita

Keyword(s):

Plasma Membrane ◽

Sequence Analysis ◽

Actin Filaments ◽

Sequence Similarity ◽

Adherens Junction ◽

Peptide Sequencing ◽

Cdna Clones ◽

Cleavage Furrow ◽

Calculated Molecular Mass ◽

Cell Biol

Radixin is an actin barbed-end capping protein which is highly concentrated in the undercoat of the cell-to-cell adherens junction and the cleavage furrow in the interphase and mitotic phase, respectively (Tsukita, Sa., Y. Hieda, and Sh. Tsukita. 1989 a.J. Cell Biol. 108:2369-2382; Sato, N., S. Yonemura, T. Obinata, Sa. Tsukita, and Sh. Tsukita. 1991. J. Cell Biol. 113:321-330). To further understand the structure and functions of the radixin molecule, we isolated and sequenced the cDNA clones encoding mouse radixin. Direct peptide sequencing of radixin and immunological analysis with antiserum to a fusion protein were performed to confirm that the protein encoded by these clones is identical to radixin. The composite cDNA is 4,241 nucleotides long and codes for a 583-amino acid polypeptide with a calculated molecular mass of 68.5 kD. Sequence analysis has demonstrated that mouse radixin shares 75.3% identity with human ezrin, which was reported to be a member of the band 4.1 family. We then isolated the cDNA encoding mouse ezrin. Sequence analysis and Northern blot analysis revealed that radixin and ezrin are similar but distinct (74.9% identity), leading us to conclude that radixin is a novel member of the band 4.1 family. In erythrocytes the band 4.1 protein acts as a key protein in the association of short actin filaments with a plasma membrane protein (glycophorin), together with spectrin. Therefore, the sequence similarity between radixin and band 4.1 protein described in this study favors the idea that radixin plays a crucial role in the association of the barbed ends of actin filaments with the plasma membrane in the cell-to-cell adherens junction and the cleavage furrow.

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Identification, sequence analysis, and characterization of cDNA clones encoding two granzyme-like serine proteinases from rat duodenum

FEBS Letters ◽

10.1016/0014-5793(93)81398-j ◽

1993 ◽

Vol 324 (2) ◽

pp. 226-230 ◽

Cited By ~ 12

Author(s):

Alexander Yu. Amerik ◽

Serge V. Yarovoi ◽

Vitali G. Grigorenko ◽

Vladimir K. Antonov

Keyword(s):

Sequence Analysis ◽

Cdna Clones ◽

Serine Proteinases ◽

Rat Duodenum

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Isolation and Molecular Characterization of a Poliovirus Type 1 Mutant That Replicates in the Spinal Cords of Mice

Journal of Virology ◽

10.1128/jvi.73.7.6041-6047.1999 ◽

1999 ◽

Vol 73 (7) ◽

pp. 6041-6047 ◽

Cited By ~ 8

Author(s):

Qingmei Jia ◽

Seii Ohka ◽

Kuniko Iwasaki ◽

Koujiro Tohyama ◽

Akio Nomoto

Keyword(s):

Spinal Cord ◽

Amino Acid ◽

Sequence Analysis ◽

Cdna Clones ◽

Mutation Site ◽

Poliovirus Type ◽

Virus Receptor ◽

Mouse Spinal Cord

ABSTRACT The Mahoney strain of poliovirus type 1 (OM) is generally unable to cause paralysis in mice. We isolated a mouse-adapted mutant, PV1/OM-SA (SA), from the spinal cord of a mouse that had been intracerebrally inoculated with OM. SA showed mouse neurovirulence only with intraspinal inoculation, and the infected mice developed a flaccid paralysis, which was indistinguishable from that observed in poliovirus-sensitive transgenic mice inoculated with OM. SA antigens were detected in neurons of the spinal cords of the infected mice. Nucleotide (nt) sequence analysis revealed 9 nt changes on the SA genome, resulting in three amino acid (a.a.) substitutions, i.e., one each in the capsid proteins VP4 and VP1 and in the noncapsid protein 2C. To identify the key mutation site(s) for the mouse neurovirulence, virus recombinants between OM and SA were constructed by using infectious cDNA clones of these two viruses and tested for their mouse neurovirulence after inoculation via an intraspinal route. The results indicated that a mutation at nt 928 (replacement of A with G), resulting in a substitution of Met for Ile at a.a. 62 within VP4, was responsible for conferring the mouse neurovirulence phenotype of the mutant SA. The mutation in VP4 may render the virus accessible to a molecule that acts as a virus receptor and is located on the surfaces of neurons of the mouse spinal cord. This molecule appears not to be expressed in the mouse brain.

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