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Titolo:
THE 24 KDA OUTER ENVELOPE MEMBRANE-PROTEIN FROM SPINACH-CHLOROPLASTS - MOLECULAR-CLONING, IN-VIVO EXPRESSION AND IMPORT PATHWAY OF A PROTEIN WITH UNUSUAL PROPERTIES
Autore:
FISCHER K; WEBER A; ARBINGER B; BRINK S; ECKERSKORN C; FLUGGE UI;
Indirizzi:
UNIV WURZBURG,JULIUS VON SACHS INST BIOWISSENSCH,MUTLERER DALLENBERGWEG 64 D-97082 WURZBURG GERMANY UNIV WURZBURG,JULIUS VON SACHS INST BIOWISSENSCH D-97082 WURZBURG GERMANY MAX PLANCK INST BIOCHEM D-82152 MARTINSRIED GERMANY
Titolo Testata:
Plant molecular biology
fascicolo: 2, volume: 25, anno: 1994,
pagine: 167 - 177
SICI:
0167-4412(1994)25:2<167:T2KOEM>2.0.ZU;2-F
Fonte:
ISI
Lingua:
ENG
Soggetto:
AMINO-ACID-SEQUENCE; PHOSPHATE TRANSLOCATOR; GEL-ELECTROPHORESIS; PRECURSOR; POLYPEPTIDES; TRANSPORT;
Keywords:
SPINACIA OLERACEA; CHEMICAL CLEAVAGE; GENE EXPRESSION; POLYMERASE CHAIN REACTION; PROTEIN TRANSPORT; SDS-PAGE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
30
Recensione:
Indirizzi per estratti:
Citazione:
K. Fischer et al., "THE 24 KDA OUTER ENVELOPE MEMBRANE-PROTEIN FROM SPINACH-CHLOROPLASTS - MOLECULAR-CLONING, IN-VIVO EXPRESSION AND IMPORT PATHWAY OF A PROTEIN WITH UNUSUAL PROPERTIES", Plant molecular biology, 25(2), 1994, pp. 167-177

Abstract

The 24 kDa outer envelope membrane protein of spinach chloroplasts (omp24) represents a major constituent of this membrane. Sequences of tryptic and endoprotease Glu-C peptides derived from omp24 allowed the design of oligonucleotides which were used to generate a DNA fragment by polymerase chain reaction using spinach cDNA as template. This fragment served as a probe to screen a cDNA library for a full-length cloneof the omp24 coding sequence. The protein predicted from the completesequence only has 148 amino acids and a molecular mass of 16294 Da. It is an acidic protein (calculated isoelectric point 4.8) with a high content of proline residues. Expression of the coding sequence in Escherichia coli and characterization of the purified recombinant protein produced revealed that the overestimation of its molecular mass by SDS-PAGE (ca. 25 kDa) is due to its abnormal amino acid composition. Despite its rather low hydrophobicity (polarity index 49%), omp24 appears to be deeply embedded in the outer membrane. Insertion of omp24 into the membrane proceeds almost independently of surface receptors or targeting sequence but, in contrast to other known outer envelope membraneproteins, is stimulated by ATP.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/04/20 alle ore 11:44:47