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Titolo:
Alternatively spliced mRNA variants of chloroplast ascorbate peroxidase isoenzymes in spinach leaves
Autore:
Yoshimura, K; Yabuta, Y; Tamoi, M; Ishikawa, T; Shigeoka, S;
Indirizzi:
Kinki Univ, Fac Agr, Dept Food & Nutr, Nara 6318505, Japan Kinki Univ Nara Japan 6318505 Agr, Dept Food & Nutr, Nara 6318505, Japan Wakayama Med Coll, Dept Biochem, Wakayama 6410012, Japan Wakayama Med Coll Wakayama Japan 6410012 iochem, Wakayama 6410012, Japan
Titolo Testata:
BIOCHEMICAL JOURNAL
, volume: 338, anno: 1999,
parte:, 1
pagine: 41 - 48
SICI:
0264-6021(19990215)338:<41:ASMVOC>2.0.ZU;2-3
Fonte:
ISI
Lingua:
ENG
Soggetto:
MESSENGER-RNA; MAIZE; EXPRESSION; EFFICIENCY; PLANTS; STRESS; RICH;
Keywords:
mRNA processing; plant mRNA; polyadenylation; post-transcriptional regulation;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
25
Recensione:
Indirizzi per estratti:
Indirizzo: Shigeoka, S Kinkipaniv, Fac Agr, Dept Food & Nutr, 3327-204 Nakamachi, Nara 6318505, Ja Kinki Univ 3327-204 Nakamachi Nara Japan 6318505 6318505, Ja
Citazione:
K. Yoshimura et al., "Alternatively spliced mRNA variants of chloroplast ascorbate peroxidase isoenzymes in spinach leaves", BIOCHEM J, 338, 1999, pp. 41-48

Abstract

We have previously shown that stromal and thylakoid-bound ascorbate peroxidase (APX) isoenzymes of spinach chloroplasts arise from a common pre-mRNA by alternative splicing in the C-terminus of the isoenzymes [Ishikawa, Yoshimura, Tamoi, Takeda and Shigeoka (1997) Biochem. J. 328, 795-800]. To explore the production of mature, functional mRNA encoding chloroplast APPX isoenzymes, reverse transcriptase-mediated PCR and S1 nuclease protection analysis were performed with poly(A)(+) RNA or polysomal RNA from spinach leaves. As a result, four mRNA variants, one form of thylakoid-bound APX (tAPX-I) and three forms of stromal APX (sAPX-I, sAPX-II and sAPX-III), were identified. The sAPX-I and sAPX-III mRNA species were generated through the excision of intron 11; they encoded the previously identified sAPX protein. Interestingly, the sAPX-II mRNA was generated by the insertion of intron 11 between exons 11 and 12. The use of this insertional sequence was in frame with the coding sequence and would lead to the production of a novel isoenzyme containing a C-terminus in which a seven-residue sequence replaced the last residue of the previously identified sAPX. The recombinant novel enzyme expressed in Escherichia coli showed the same enzymic properties (except for molecular mass) as the recombinant sAPX from the previously identified sAPX-I mRNA, suggesting that the protein translated from the sAPX-II mRNA is functional as a soluble APX in vivo. The S1 nuclease protection analysis showed that the expression levels of mRNA variants for sAPX and tAPX isoenzymes are in nearly equal quantities throughout the spinach leaves grown undernormal conditions. The present results demonstrate that the expression of chloroplast APX isoenzymes is regulated by a differential splicing efficiency that is dependent on the 3'-terminal processing of ApxII, the gene encoding the chloroplast APX isoenzymes.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 30/11/20 alle ore 07:21:03