Transfer of methionyl residues by leucyl, phenylalanyl-tRNA-protein transferase

R. C. Scarpulla; C. E. Deutch; R. L. Soffer

doi:10.1016/0006-291X(76)90827-5

Transfer of methionyl residues by leucyl, phenylalanyl-tRNA-protein transferase

R. C. Scarpulla^*, C. E. Deutch, R. L. Soffer

^*Corresponding author for this work

Cell & Developmental Biology

Research output: Contribution to journal › Article › peer-review

23 Scopus citations

Abstract

Leucyl, phenylalanyl-tRNA-protein transferase also catalyzes transfer of methionyl residues as indicated by (i) copurification over a 1000-fold range of transfer activities for all three amino acids and (ii) loss of methionyl transfer activity in a mutant of E. coli lacking the transferase and reappearance of this activity in a transferase revertant. The purified enzyme was found to use Met-tRNA_m^Met in preference to Met-tRNA_f^Met as donor substrate. Peptides containing a basic amino acid at the NH₂-terminus functioned as acceptors for the transfer of methionyl residues.

Original language	English (US)
Pages (from-to)	584-589
Number of pages	6
Journal	Biochemical and Biophysical Research Communications
Volume	71
Issue number	2
DOIs	https://doi.org/10.1016/0006-291X(76)90827-5
State	Published - Jul 26 1976

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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10.1016/0006-291X(76)90827-5

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title = "Transfer of methionyl residues by leucyl, phenylalanyl-tRNA-protein transferase",

abstract = "Leucyl, phenylalanyl-tRNA-protein transferase also catalyzes transfer of methionyl residues as indicated by (i) copurification over a 1000-fold range of transfer activities for all three amino acids and (ii) loss of methionyl transfer activity in a mutant of E. coli lacking the transferase and reappearance of this activity in a transferase revertant. The purified enzyme was found to use Met-tRNAmMet in preference to Met-tRNAfMet as donor substrate. Peptides containing a basic amino acid at the NH2-terminus functioned as acceptors for the transfer of methionyl residues.",

author = "Scarpulla, {R. C.} and Deutch, {C. E.} and Soffer, {R. L.}",

note = "Funding Information: We thank Dr. LaDonne Schulman for the preparations of tRNAMet and t*t. This work was supported by a grant from the National s cience Foundation (BHS 74-23970). R.C.S. is a Predoctoral Trainee of the National Institutes of Health (IT-32-GM-07128). C.&D. is a Mellon Fellow. R.L.S. is a Faculty Research Associate of the American Cancer Society.",

year = "1976",

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doi = "10.1016/0006-291X(76)90827-5",

language = "English (US)",

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pages = "584--589",

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T1 - Transfer of methionyl residues by leucyl, phenylalanyl-tRNA-protein transferase

AU - Scarpulla, R. C.

AU - Deutch, C. E.

AU - Soffer, R. L.

N1 - Funding Information: We thank Dr. LaDonne Schulman for the preparations of tRNAMet and t*t. This work was supported by a grant from the National s cience Foundation (BHS 74-23970). R.C.S. is a Predoctoral Trainee of the National Institutes of Health (IT-32-GM-07128). C.&D. is a Mellon Fellow. R.L.S. is a Faculty Research Associate of the American Cancer Society.

PY - 1976/7/26

Y1 - 1976/7/26

N2 - Leucyl, phenylalanyl-tRNA-protein transferase also catalyzes transfer of methionyl residues as indicated by (i) copurification over a 1000-fold range of transfer activities for all three amino acids and (ii) loss of methionyl transfer activity in a mutant of E. coli lacking the transferase and reappearance of this activity in a transferase revertant. The purified enzyme was found to use Met-tRNAmMet in preference to Met-tRNAfMet as donor substrate. Peptides containing a basic amino acid at the NH2-terminus functioned as acceptors for the transfer of methionyl residues.

AB - Leucyl, phenylalanyl-tRNA-protein transferase also catalyzes transfer of methionyl residues as indicated by (i) copurification over a 1000-fold range of transfer activities for all three amino acids and (ii) loss of methionyl transfer activity in a mutant of E. coli lacking the transferase and reappearance of this activity in a transferase revertant. The purified enzyme was found to use Met-tRNAmMet in preference to Met-tRNAfMet as donor substrate. Peptides containing a basic amino acid at the NH2-terminus functioned as acceptors for the transfer of methionyl residues.

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Transfer of methionyl residues by leucyl, phenylalanyl-tRNA-protein transferase

Abstract

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