Are Vitellin and Vitellogenin Coded by One Gene in the Marine Shrimp Penaeus semisulcatus?

1994 ◽  
Vol 12 (2) ◽  
pp. 251-254 ◽  
Author(s):  
M Khayat ◽  
E Lubzens ◽  
A Tietz ◽  
B Funkenstein

ABSTRACT A cDNA clone encoding a female-specific ovarian protein (presumably vitellin, Vt) has been isolated from a cDNA library prepared from poly (A)+ RNA extracted from vitellogenic ovaries of the shrimp Penaeus semisulcatus. The cDNA library was constructed and screened using a major cDNA band which was observed following analysis of total cDNA products by gel electrophoresis. This band, as well as the cDNA insert purified from the library, was estimated to have 1.1 kb. Both hybridized to mRNA prepared from ovaries or hepatopancreas (HEP) of vitellogenic females and showed a faint signal with ovaries from non-vitellogenic females, but did not hybridize to HEP from non-vitellogenic females or to HEP from males or testes. The size of the transcripts from the ovary and HEP was estimated to be 1.1 kb, similar to that of the cDNA insert, suggesting that a full length cDNA had been synthesized. Furthermore, the identical sizes of the transcripts from ovary and HEP and the ability of the ovarian cDNA to detect a transcript in HEP mRNA suggest that Vt from the ovary and vitellogenin (Vg) from HEP are the gene products of one gene. Alternatively, the homology between Vt and Vg is very high.

1991 ◽  
Vol 276 (2) ◽  
pp. 337-342 ◽  
Author(s):  
K Ohkubo ◽  
S Ogata ◽  
Y Misumi ◽  
N Takami ◽  
H Sinohara ◽  
...  

A cDNA clone (lambda MC-2) for contrapsin, a serine-proteinase inhibitor, was isolated from a lambda ZAP mouse liver cDNA library. The 1.6 kb cDNA insert of lambda MC-2 contained an open reading frame that encodes a 418-residue polypeptide (46,970 Da), in which a signal peptide of 21 residues was identified by comparison with the N-terminal sequence of the purified protein. The predicted structure (MC-2) also contained other peptide sequences determined by Edman degradation. Four potential sites for N-linked glycosylation were found in the molecule, accounting for the difference in molecular mass between the predicted form and the purified protein (63 kDa). Further screening of the cDNA library with an EcoRI-EcoRI fragment (510 bp) of lambda MC-2 as a probe yielded another cDNA clone (lambda MC-7), which encodes a 418-residue polypeptide (MC-7) with a calculated mass of 47,010 Da. MC-2 showed 83% similarity at the amino acid level to MC-7, in contrast with 44% similarity to alpha 1-proteinase inhibitor. The possible reactive site (P1-P'1) for serine proteinase is suggested to be Lys-Ala for MC-2 and Ser-Arg for MC-7. Northern-blot analysis revealed that both MC-2 and MC-7 mRNAs have the same size of 1.8 kb and are markedly induced in response to acute inflammation. Construction of the expression plasmids pSVMC-2 and pSVMC-7 and their transfection into COS-1 cells demonstrated that pSVMC-2 directs the synthesis of a 63 kDa form whereas pSVMC-7 expresses a 56 kDa form. The difference in molecular mass between the two may be explained by the fact that the MC-7 sequence contains three potential sites for N-glycosylation, one site less than that of MC-2.


2009 ◽  
Vol 35 (4) ◽  
pp. 602-607 ◽  
Author(s):  
Dong WU ◽  
Jun-Jie LIU ◽  
Shu-Xun YU ◽  
Shu-Li FAN ◽  
Mei-Zhen SONG

2021 ◽  
Vol 166 (5) ◽  
pp. 1427-1431
Author(s):  
Buyang Chen ◽  
Qi Lin ◽  
Yueyan Yin ◽  
Liangliang Jiang ◽  
Fang Wang ◽  
...  

2008 ◽  
Vol 74 (6) ◽  
pp. 434-437 ◽  
Author(s):  
Atsushi Ohkawa ◽  
Noriko Ishikawa-Suehiro ◽  
Seiichi Okuda ◽  
Tomohide Natsuaki

2011 ◽  
Vol 10 (1) ◽  
pp. 28-40 ◽  
Author(s):  
Li-na WANG ◽  
Dong WU ◽  
Shu-xun YU ◽  
Shu-li FAN ◽  
Mei-zhen SONG ◽  
...  

1986 ◽  
Vol 6 (8) ◽  
pp. 3018-3022
Author(s):  
B D Tong ◽  
S E Levine ◽  
M Jaye ◽  
G Ricca ◽  
W Drohan ◽  
...  

A clone containing the 3' end of the mRNA for the human c-sis gene (homologous to the B chain of platelet-derived growth factor) was isolated from a cDNA library derived from human umbilical vein endothelial cells and then sequenced. The analysis of possible translation products in all three reading frames indicated that the A chain of platelet-derived growth factor was not coded for within the 3' end of the c-sis mRNA. The 3' end of the mRNA for c-sis is contained in or adjacent to exon 6.


1985 ◽  
Vol 5 (10) ◽  
pp. 2697-2704
Author(s):  
L J Lorenz ◽  
J D Richter

Xenopus laevis oocytes contain a unique group of proteins which decrease during oogenesis, bind poly(A) RNA, and possibly play a role in the regulation of translation. A monoclonal antibody generated against one of these proteins was used to screen an expression vector cDNA library. A cDNA clone was isolated and confirmed to code for the binding protein by in vitro translation of hybrid-selected RNA followed by immunoprecipitation. This cDNA, when used in RNA gel blots, hybridized to four transcripts of 2.0, 1.7 (two transcripts of similar size), and 1.2 kilobases. All of the transcripts decreased in amount during oogenesis and were not evident in somatic cells. In addition, the fraction of the transcripts associated with polysomes decreased during oogenesis. Digestion of the cDNA insert with PstI generated two fragments of 220 and 480 base pairs which, when used as probes in an RNA gel blot, hybridized to unique as well as common transcripts. Genomic Southern blots suggested the presence of a single gene, indicating that these transcripts arose by alternative processing.


2014 ◽  
Vol 13 (2) ◽  
pp. 378-386
Author(s):  
Su-mei ZHAO ◽  
Yong-gang LIU ◽  
Hong-bing PAN ◽  
Xi ZHANG ◽  
Chang-rong GE ◽  
...  

1987 ◽  
Vol 15 (16) ◽  
pp. 6740-6740 ◽  
Author(s):  
Hans-Jürgen Schmelzer ◽  
Gerhard Gross ◽  
Georg Widera ◽  
Hubert Mayer

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