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Titolo:
CLONING OF A CDNA-ENCODING PHOSPHOLIPASE-D FROM PIMPINELLA-BRACHYCARPA
Autore:
CHA YR; LEE KW; MOON YH; KIN JC; HAN TJ; LEE WS; CHO SH;
Indirizzi:
INHA UNIV,DEPT BIOL INCHON 402751 SOUTH KOREA INHA UNIV,DEPT BIOL INCHON 402751 SOUTH KOREA SEOUL NATL UNIV,DEPT BIOL SEOUL 151742 SOUTH KOREA KANGWEON NATL UNIV,DEPT BIOL CHUNCHON 200701 SOUTH KOREA HALLYM UNIV,DEPT BIOL CHUNCHON 200702 SOUTH KOREA SUNG KYUN KWAN UNIV,DEPT BIOL SUWON 440746 SOUTH KOREA
Titolo Testata:
Molecules and cells
fascicolo: 1, volume: 8, anno: 1998,
pagine: 19 - 26
SICI:
1016-8478(1998)8:1<19:COACPF>2.0.ZU;2-H
Fonte:
ISI
Lingua:
ENG
Soggetto:
PLANTS; ALIGNMENT; FAMILY; DOMAIN; DELTA;
Keywords:
P-BRACHYCARPA; PHOSPHOLIPASE D; MEMBRANE; SIGNAL TRANSDUCTION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
33
Recensione:
Indirizzi per estratti:
Citazione:
Y.R. Cha et al., "CLONING OF A CDNA-ENCODING PHOSPHOLIPASE-D FROM PIMPINELLA-BRACHYCARPA", Molecules and cells, 8(1), 1998, pp. 19-26

Abstract

Phospholipase D (PLD, EC 3.1.4.4) has been known to be related to various cellular processes in plants. To gain an understanding of the property of the enzyme in Pimpinella brachycarpa, the cDNA of the enzyme was isolated by PCR with degenerate primers, cDNA library screening, and 5' RACE. The full-length PLD cDNA is 2859 bp long and contains an open reading frame of 2424 bp coding for a polypeptide of 808 amino acids. The deduced enzyme has a calculated molecular mass of 91.7 kDa andpi of 5.86, The percent identity and similarity values of P. brachycarpa PLD with those of other PLDs in plants are 70 similar to 78 and 84similar to 95, respectively. It was identified that PLD from P. brachycarpa has HQKIVVVD and HAKMMIVD sequences which were homologous with a duplicated HXKXXXXD motif that has been conserved in PLDs from plants, animals, and yeast, Based on the analysis of amino acid similarity,it is believed that PLD from P. brachycarpa is an alpha form which isdistinct from PLD beta reported recently. The N-terminus is homologous to the C2 domain which is present in a number of different proteins involved in signal transduction and membrane trafficking in animals. Southern and northern blot analyses indicated that PLD was expressed from one copy of PLD gene in the genome of P. brachycarpa.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 28/11/20 alle ore 09:54:56