Cytoplasmic leucyl-tRNA synthetase of Neurospora crassa is not specified by the leu-5 locus.

نویسندگان

  • R Benarous
  • C M Chow
  • U L RajBhandary
چکیده

We generated a lambda gt11 Neurospora crassa cDNA library and screened the library for the cytoplasmic leucyl-tRNA synthetase (cyto LeuRS) clones using cyto LeuRS specific antibody. Two clones, lambda NCLRSC1 and lambda NCLRSC2, were obtained which have inserts of approximately 2 kbp and approximately 1.3 kbp, and which overlap by about 0.6 kbp. The following lines of evidence indicate that lambda NCLRSC1 and lambda NCLRSC2 encode parts of cyto LeuRS. (1) Antibodies affinity purified using either of the fusion proteins encoded by lambda NCLRSC1 or lambda NCLRSC2 inhibit cyto LeuRS activity. Thus, the fusion protein and cyto LeuRS share immunological determinants. (2) The same antibodies also react with an approximately 115-kDa protein, which comigrates with purified cyto LeuRS, in immunoblots of total N. crassa proteins. We used the cDNA clones to probe a N. crassa genomic DNA library and isolated two genomic DNA clones. Partial sequence analysis of cDNA and genomic DNA clones shows a methionine initiated open reading frame, which includes a stretch of amino acid residues that are highly conserved and that are at the ATP binding site in aminoacyl-tRNA synthetases. Using the cloned DNA as probe, we show that the cyto LeuRS mRNA is approximately 3900 nucleotides long. Finally, we have used restriction fragment length polymorphism mapping to show that the cyto LeuRS gene resides on the far right of linkage group II and not on linkage group V where the leu-5 mutation, which was previously reported to specify cyto LeuRS, is located.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Interactions of Phenylalanyl Transfer Ribonucleic Acid Synthetase of Neurospora crassa with Valyl Transfer Ribonucleic Acid of Escherichia co&*

Since Phe-tRNA synthetase of Neurospora crassa reacts with tRNAV”’ of Escherichia coli to produce Phe-tRNAV&‘, the parameters that effect the reverse reaction were examined. Similarly, the interaction of Val-tRNA synthetase (E. coti) with Phe-tRNAVal and Val-tRNAVal (E. coli) was studied. Phe-tRNA synthetase (N. crassa) can catalyze the deacylation of both Phe-tRNAVa 1 (E. coli) and Val-tRNAV”’...

متن کامل

Interactions of Phenylalanyl Transfer Ribonucleic Acid Synthetase of Neurospora crassa with Valyl Transfer Ribonucleic Acid of Escherichia co&*

Since Phe-tRNA synthetase of Neurospora crassa reacts with tRNAV”’ of Escherichia coli to produce Phe-tRNAV&‘, the parameters that effect the reverse reaction were examined. Similarly, the interaction of Val-tRNA synthetase (E. coti) with Phe-tRNAVal and Val-tRNAVal (E. coli) was studied. Phe-tRNA synthetase (N. crassa) can catalyze the deacylation of both Phe-tRNAVa 1 (E. coli) and Val-tRNAV”’...

متن کامل

Interactions of phenylalanyl transfer ribonucleic acid synthetase of Neurospora crassa with valyl transfer ribonucleic acid of Escherichia coli.

Since Phe-tRNA synthetase of Neurospora crassa reacts with tRNAV”’ of Escherichia coli to produce Phe-tRNAV&‘, the parameters that effect the reverse reaction were examined. Similarly, the interaction of Val-tRNA synthetase (E. coti) with Phe-tRNAVal and Val-tRNAVal (E. coli) was studied. Phe-tRNA synthetase (N. crassa) can catalyze the deacylation of both Phe-tRNAVa 1 (E. coli) and Val-tRNAV”’...

متن کامل

Evidence for the involvement of a nuclear gene in the productin of the mitochondrial leucyl-tRNA synthetase of Neurospora.

The mitochondria of Neurospora have been shown to contain many elements of the machinery of protein synthesis that are distinctly different from those of the rest of the cell. The differences observed in the structural and functional specificity of mitochondrial and "cytoplasmic" ribosomes,I transfer RNA's,2 and several aminoacyl-tRNA synthetases3 suggest that protein synthesis in mitochondria ...

متن کامل

An apparent relationship between mistranslation and an altered leucyl-tRNA synthetase in a conditional lethal mutant of Neurospora crassa.

A N analysis of the genetic control of the biogenesis of leucine biosynthetic enzymes in Neurospora crussu has established that four cistrons are involved in the determination o F the structures of the three enzymes specifically responsible for the formation of leucine (GROSS 1965). However, the function of a fifth cistron, leu-5 represent'ed by a single mutant strain, 45208t, remained enigmati...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:
  • Genetics

دوره 119 4  شماره 

صفحات  -

تاریخ انتشار 1988