Cloning and characterization of a developmentally regulated sea urchin cDNA encoding glutamine synthetase

Laura Fucci; Annamaria Piscopo; Francesco Aniello; Margherita Branno; Anna Di Gregorio; Raffaele Calogero; Giuseppe Geraci

doi:10.1016/0378-1119(94)00719-9

Cloning and characterization of a developmentally regulated sea urchin cDNA encoding glutamine synthetase

Laura Fucci, Annamaria Piscopo, Francesco Aniello, Margherita Branno, Anna Di Gregorio, Raffaele Calogero, Giuseppe Geraci

Molecular Pathobiology

Research output: Contribution to journal › Article › peer-review

Abstract

A 2935-bp cDNA clone encoding glutamine synthetase (GS) was isolated from a cDNA library prepared from four-blastomere Paracentrotus lividus sea urchin embryos. The sequence consists of a 75-bp 5′ untranslated region (5′-UTR) followed by a 1095-bp coding region corresponding to a 365-amino-acid (aa) protein, a 1747-bp 3′-UTR and a terminal 18-bp poly(A) tail. The encoded protein shows about 66% identical residues, as compared with human and lobster class-II GS. The sequence contains the Mn²⁺-binding aa and the highly conserved aa regions observed in other GS. Northern blot analyses show that the GS mRNA is present in the sea urchin egg and is developmentally regulated in the embryo.

Original language	English (US)
Pages (from-to)	205-208
Number of pages	4
Journal	Gene
Volume	152
Issue number	2
DOIs	https://doi.org/10.1016/0378-1119(94)00719-9
State	Published - Jan 23 1995

Keywords

Paracentrotus lividus
Recombinant DNA
comparison with human and lobster GS
embryo
mRNA control

ASJC Scopus subject areas

Genetics

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10.1016/0378-1119(94)00719-9

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title = "Cloning and characterization of a developmentally regulated sea urchin cDNA encoding glutamine synthetase",

abstract = "A 2935-bp cDNA clone encoding glutamine synthetase (GS) was isolated from a cDNA library prepared from four-blastomere Paracentrotus lividus sea urchin embryos. The sequence consists of a 75-bp 5′ untranslated region (5′-UTR) followed by a 1095-bp coding region corresponding to a 365-amino-acid (aa) protein, a 1747-bp 3′-UTR and a terminal 18-bp poly(A) tail. The encoded protein shows about 66% identical residues, as compared with human and lobster class-II GS. The sequence contains the Mn2+-binding aa and the highly conserved aa regions observed in other GS. Northern blot analyses show that the GS mRNA is present in the sea urchin egg and is developmentally regulated in the embryo.",

keywords = "Paracentrotus lividus, Recombinant DNA, comparison with human and lobster GS, embryo, mRNA control",

author = "Laura Fucci and Annamaria Piscopo and Francesco Aniello and Margherita Branno and {Di Gregorio}, Anna and Raffaele Calogero and Giuseppe Geraci",

note = "Funding Information: Work supported in part by the 60% and 40% funds of the Italian Ministero dell'Universit/t e della Ricerca Scientifica e Tecnologica.",

year = "1995",

month = jan,

day = "23",

doi = "10.1016/0378-1119(94)00719-9",

language = "English (US)",

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pages = "205--208",

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T1 - Cloning and characterization of a developmentally regulated sea urchin cDNA encoding glutamine synthetase

AU - Fucci, Laura

AU - Piscopo, Annamaria

AU - Aniello, Francesco

AU - Branno, Margherita

AU - Di Gregorio, Anna

AU - Calogero, Raffaele

AU - Geraci, Giuseppe

N1 - Funding Information: Work supported in part by the 60% and 40% funds of the Italian Ministero dell'Universit/t e della Ricerca Scientifica e Tecnologica.

PY - 1995/1/23

Y1 - 1995/1/23

N2 - A 2935-bp cDNA clone encoding glutamine synthetase (GS) was isolated from a cDNA library prepared from four-blastomere Paracentrotus lividus sea urchin embryos. The sequence consists of a 75-bp 5′ untranslated region (5′-UTR) followed by a 1095-bp coding region corresponding to a 365-amino-acid (aa) protein, a 1747-bp 3′-UTR and a terminal 18-bp poly(A) tail. The encoded protein shows about 66% identical residues, as compared with human and lobster class-II GS. The sequence contains the Mn2+-binding aa and the highly conserved aa regions observed in other GS. Northern blot analyses show that the GS mRNA is present in the sea urchin egg and is developmentally regulated in the embryo.

AB - A 2935-bp cDNA clone encoding glutamine synthetase (GS) was isolated from a cDNA library prepared from four-blastomere Paracentrotus lividus sea urchin embryos. The sequence consists of a 75-bp 5′ untranslated region (5′-UTR) followed by a 1095-bp coding region corresponding to a 365-amino-acid (aa) protein, a 1747-bp 3′-UTR and a terminal 18-bp poly(A) tail. The encoded protein shows about 66% identical residues, as compared with human and lobster class-II GS. The sequence contains the Mn2+-binding aa and the highly conserved aa regions observed in other GS. Northern blot analyses show that the GS mRNA is present in the sea urchin egg and is developmentally regulated in the embryo.

KW - Paracentrotus lividus

KW - Recombinant DNA

KW - comparison with human and lobster GS

KW - embryo

KW - mRNA control

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U2 - 10.1016/0378-1119(94)00719-9

DO - 10.1016/0378-1119(94)00719-9

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C2 - 7835701

AN - SCOPUS:0028910282

SN - 0378-1119

VL - 152

SP - 205

EP - 208

JO - Gene

JF - Gene

IS - 2

ER -

Cloning and characterization of a developmentally regulated sea urchin cDNA encoding glutamine synthetase

Abstract

Keywords

ASJC Scopus subject areas

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