OCCURRENCE OF A COPIA-LIKE TRANSPOSABLE ELEMENT IN ONE OF THE INTRONS OF THE POTATO STARCH PHOSPHORYLASE GENE

被引:56
作者
CAMIRAND, A [1 ]
STPIERRE, B [1 ]
MARINEAU, C [1 ]
BRISSON, N [1 ]
机构
[1] UNIV MONTREAL, DEPT BIOCHEM, MONTREAL H3C 3J7, QUEBEC, CANADA
来源
MOLECULAR AND GENERAL GENETICS | 1990年 / 224卷 / 01期
关键词
Retrotransposon; Reverse transcriptase; Solanum tuberosum; Tuber;
D O I
10.1007/BF00259448
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The gene coding for starch phosphorylase (EC 2.4.1.1) was isolated from a potato genomic library constructed in λEMBL3. It is an unusually long plant gene (16.4 kb) which encodes a preprotein of 966 amino acids. The phosphorylase coding sequence is interrupted by 14 introns whose positions do not match those of the introns in the human glycogen phosphorylase gene. A 78 amino acid central peptide unique to plant plastidial phosphorylases is hypothesized to have arisen through the mis-splicing of an intron-exon junction site in an ancestral gene. The fifth intron of the phosphorylase is very large (approximately 7 kb) and contains a copia-like transposable element inserted in the opposite orientation to that of the phosphorylase gene. This element has been named Tstl ; it is bordered on the 5′ and 3′ sides by long terminal repeats of 285 and 283 bp respectively, which define an internal domain of 4492 bp. Tstl contains 4 open reading frames (ORFs) that encode protein domains for a reverse transcriptase, an integrase, an RNA-binding site and a protease. Transcription of the phosphorylase gene appears to proceed unimpaired through the copia element. © 1990 Springer-Verlag.
引用
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页码:33 / 39
页数:7
相关论文
共 39 条
[1]  
BREATHNACH R, 1981, ANNU REV BIOCHEM, V50, P349, DOI 10.1146/annurev.bi.50.070181.002025
[2]   MATURATION AND SUBCELLULAR COMPARTMENTATION OF POTATO STARCH PHOSPHORYLASE [J].
BRISSON, N ;
GIROUX, H ;
ZOLLINGER, M ;
CAMIRAND, A ;
SIMARD, C .
PLANT CELL, 1989, 1 (05) :559-566
[3]   INTRON EXON STRUCTURE OF THE HUMAN-GENE FOR THE MUSCLE ISOZYME OF GLYCOGEN-PHOSPHORYLASE [J].
BURKE, J ;
HWANG, P ;
ANDERSON, L ;
LEBO, R ;
GORIN, F ;
FLETTERICK, R .
PROTEINS-STRUCTURE FUNCTION AND GENETICS, 1987, 2 (03) :177-187
[4]   PURIFICATION AND PROPERTIES OF GLYCOGEN PHOSPHORYLASE FROM ESCHERICHIA COLI [J].
CHEN, GS ;
SEGEL, IH .
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 1968, 127 (1-3) :175-&
[5]   NUCLEOTIDE-SEQUENCE OF A YEAST TY ELEMENT - EVIDENCE FOR AN UNUSUAL MECHANISM OF GENE-EXPRESSION [J].
CLARE, J ;
FARABAUGH, P .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1985, 82 (09) :2829-2833
[6]   MOLECULAR ANALYSIS OF THE ALCOHOL DEHYDROGENASE-2 (ADH2) GENE OF MAIZE [J].
DENNIS, ES ;
SACHS, MM ;
GERLACH, WL ;
FINNEGAN, EJ ;
PEACOCK, WJ .
NUCLEIC ACIDS RESEARCH, 1985, 13 (03) :727-743
[7]   MOLECULAR ANALYSIS OF THE ALCOHOL-DEHYDROGENASE (ADHL) GENE OF MAIZE [J].
DENNIS, ES ;
GERLACH, WL ;
PRYOR, AJ ;
BENNETZEN, JL ;
INGLIS, A ;
LLEWELLYN, D ;
SACHS, MM ;
FERL, RJ ;
PEACOCK, WJ .
NUCLEIC ACIDS RESEARCH, 1984, 12 (09) :3983-4000
[8]   ORIGINS AND EVOLUTIONARY RELATIONSHIPS OF RETROVIRUSES [J].
DOOLITTLE, RF ;
FENG, DF ;
JOHNSON, MS ;
MCCLURE, MA .
QUARTERLY REVIEW OF BIOLOGY, 1989, 64 (01) :1-30
[9]   A PLANT PROCESSED PSEUDOGENE [J].
DROUIN, G ;
DOVER, GA .
NATURE, 1987, 328 (6130) :557-558
[10]   PURIFICATION AND PROPERTIES OF YEAST GLYCOGEN PHOSPHORYLASE-A AND B [J].
FOSSET, M ;
MUIR, LW ;
NIELSEN, LD ;
FISCHER, EH .
BIOCHEMISTRY, 1971, 10 (22) :4105-+