EVIDENCE OF SELECTION FOR PROTEIN INTRONS IN THE RECAS OF PATHOGENIC MYCOBACTERIA

被引:96
作者
DAVIS, EO
THANGARAJ, HS
BROOKS, PC
COLSTON, MJ
机构
[1] Lab. Leprosy and Mycobacterial Res., Natl. Institute for Medical Research, The Ridgeway, London NW7 1AA, Mill Hill
关键词
LEPROSY; MYCOBACTERIA; PROTEIN INTRON; PROTEIN SPLICING; TUBERCULOSIS;
D O I
10.1002/j.1460-2075.1994.tb06309.x
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
Protein introns are recently discovered genetic elements whose intervening sequences are removed from a precursor protein by an unusual protein splicing reaction. This involves the excision of a central spacer molecule, the protein intron, and the religation of the amino- and carboxy-terminal fragments of the precursor. The recA gene of Mycobacterium tuberculosis contains one such element and we now show that the other major mycobacterial pathogen, Mycobacterium leprae, also possesses a protein intron in its recA, although other mycobacterial recA genes do not. However, these two protein introns are different in size, sequence and location of insertion of their coding sequences into the recAs of M.tuberculosis and M.leprae, indicating that acquisition of the protein introns has occurred independently in the two species, and thus suggesting that there has been selection for splicing in the maturation of RecA in the pathogenic mycobacteria. The M.leprae protein intron provides an example of conditional protein splicing, splicing occurring in M.leprae itself but not when expressed in Escherichia coli, unlike most previously described protein introns. These observations suggest that protein introns may perform a function for their host, rather than being just selfish elements.
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页码:699 / 703
页数:5
相关论文
共 21 条
[1]   PROTEIN SPLICING OF THE YEAST TFP1 INTERVENING PROTEIN-SEQUENCE - A MODEL FOR SELF-EXCISION [J].
COOPER, AA ;
CHEN, YJ ;
LINDORFER, MA ;
STEVENS, TH .
EMBO JOURNAL, 1993, 12 (06) :2575-2583
[2]   PROTEIN SPLICING IN THE MATURATION OF MYCOBACTERIUM-TUBERCULOSIS RECA PROTEIN - A MECHANISM FOR TOLERATING A NOVEL CLASS OF INTERVENING SEQUENCE [J].
DAVIS, EO ;
JENNER, PJ ;
BROOKS, PC ;
COLSTON, MJ ;
SEDGWICK, SG .
CELL, 1992, 71 (02) :201-210
[3]   NOVEL STRUCTURE OF THE RECA LOCUS OF MYCOBACTERIUM-TUBERCULOSIS IMPLIES PROCESSING OF THE GENE-PRODUCT [J].
DAVIS, EO ;
SEDGWICK, SG ;
COLSTON, MJ .
JOURNAL OF BACTERIOLOGY, 1991, 173 (18) :5653-5662
[4]   A COMPREHENSIVE SET OF SEQUENCE-ANALYSIS PROGRAMS FOR THE VAX [J].
DEVEREUX, J ;
HAEBERLI, P ;
SMITHIES, O .
NUCLEIC ACIDS RESEARCH, 1984, 12 (01) :387-395
[6]   USE OF AN ORDERED COSMID LIBRARY TO DEDUCE THE GENOMIC ORGANIZATION OF MYCOBACTERIUM-LEPRAE [J].
EIGLMEIER, K ;
HONORE, N ;
WOODS, SA ;
CAUDRON, B ;
COLE, ST .
MOLECULAR MICROBIOLOGY, 1993, 7 (02) :197-206
[7]   HOMING OF A DNA ENDONUCLEASE GENE BY MEIOTIC GENE CONVERSION IN SACCHAROMYCES-CEREVISIAE [J].
GIMBLE, FS ;
THORNER, J .
NATURE, 1992, 357 (6376) :301-306
[8]  
GU HH, 1993, J BIOL CHEM, V268, P7372
[9]   MUTATIONS AT THE PUTATIVE JUNCTION SITES OF THE YEAST VMA1 PROTEIN, THE CATALYTIC SUBUNIT OF THE VACUOLAR MEMBRANE H+-ATPASE, INHIBIT ITS PROCESSING BY PROTEIN SPLICING [J].
HIRATA, R ;
ANRAKU, Y .
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 1992, 188 (01) :40-47
[10]  
HIRATA R, 1990, J BIOL CHEM, V265, P6726