Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
A FAMILY OF POTATO GENES THAT ENCODE KUNITZ-TYPE PROTEINASE-INHIBITORS - STRUCTURAL COMPARISONS AND DIFFERENTIAL EXPRESSION
Autore:
ISHIKAWA A; OHTA S; MATSUOKA K; HATTORI T; NAKAMURA K;
Indirizzi:
NAGOYA UNIV,SCH AGR,BIOCHEM LAB,CHIKUSA KU NAGOYA 46401 JAPAN NAGOYA UNIV,SCH AGR,BIOCHEM LAB,CHIKUSA KU NAGOYA 46401 JAPAN
Titolo Testata:
Plant and Cell Physiology
fascicolo: 2, volume: 35, anno: 1994,
pagine: 303 - 312
SICI:
0032-0781(1994)35:2<303:AFOPGT>2.0.ZU;2-T
Fonte:
ISI
Lingua:
ENG
Soggetto:
MAJOR SOLUBLE-PROTEIN; HIGH-LEVEL EXPRESSION; ROOT STORAGE PROTEIN; AMINO-ACID-SEQUENCE; SOLANUM-TUBEROSUM L; SWEET-POTATO; TRYPSIN-INHIBITOR; INDUCIBLE EXPRESSION; NUCLEOTIDE-SEQUENCE; MOLECULAR-CLONING;
Keywords:
JASMONATE; KUNITZ-TYPE PROTEINASE INHIBITOR; MULTIGENE FAMILY; SOLANUM-TUBEROSUM;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
34
Recensione:
Indirizzi per estratti:
Citazione:
A. Ishikawa et al., "A FAMILY OF POTATO GENES THAT ENCODE KUNITZ-TYPE PROTEINASE-INHIBITORS - STRUCTURAL COMPARISONS AND DIFFERENTIAL EXPRESSION", Plant and Cell Physiology, 35(2), 1994, pp. 303-312

Abstract

Potato tubers contain a complex group of proteins of 20 to 24 kDa that exhibit homology to Kunitz-type proteinase inhibitors. We isolated three cDNAs and two genomic clones that encode members of the potato Kunitz-type proteinase inhibitor (PKPI) family. Comparison of the structures of these and other cloned genes indicated that genes of the PKPI family can be classified into three major homology groups, namely, A, B and C. The PKPI-A and -B genes exhibit higher homology to one another than to the PKPI-C genes. Determination of the N-terminal amino acidsequences of 18 polypeptides from the complex group of 20- to 24-kDa proteins that had been separated by column chromatography and subsequently gel electrophoresis revealed three different sequences that corresponded to PKPI-A, -B, and -C. PKPI-A genes include those coding for acathepsin D inhibitor, while PKPI-B and -C genes include those codingfor trypsin and/or chymotrypsin inhibitors and a subtilisin inhibitor. Precursors to PKPIs are synthesized with an N-terminal extra peptidethat appears to contain, in addition to the signal peptide, a short propeptide with a highly conserved Asn-Pro-Ile-Xxx-Leu-Pro motif that is identical to the potential vacuolar-sorting determinant in the N-terminal propeptide of a precursor to sporamin of sweet potato. Expression of the PKPI-A and -B genes is differentially regulated: PKPI-A mRNA but not PKPI-B mRNA were induced in leaves after wounding or upon treatment with methyl jasmonate. Nuclear genes for PKPI-A and -B do not contain introns, and the homology between the two types of gene extends only 72 bp upstream from the site of initiation of transcription.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 01/12/20 alle ore 07:26:52