Protein chain initiation by methionyl-tRNA

Jonathan P. Leis; Elizabeth B. Keller

doi:10.1016/0006-291X(70)91025-9

Protein chain initiation by methionyl-tRNA

Jonathan P. Leis^*, Elizabeth B. Keller

^*Corresponding author for this work

Microbiology-Immunology

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

50 Scopus citations

Abstract

Wheat germ contains three chromatographically distinct methionine tRNA's, of which two species, one major and one minor, appear to function in protein chain initiation as demonstrated by the AUG-dependent reaction with puromycin on wheat germ ribosomes. Wheat germ extracts contain a very active transformylase which formylates the minor methionyl-tRNA. The major initiating methionyl-tRNA is not formylated or otherwise modified by wheat germ extracts. We postulate that protein chain initiation in the cytoplasm of wheat germ can be brought about by the major initiating methionyl-tRNA without prior formylation or other modification of the α amino group.

Original language	English (US)
Pages (from-to)	416-421
Number of pages	6
Journal	Biochemical and Biophysical Research Communications
Volume	40
Issue number	2
DOIs	https://doi.org/10.1016/0006-291X(70)91025-9
State	Published - Jul 27 1970

Funding

We wish to thank Mrs. Clara T. Kahn for invaluable assistance in these experiments, Dr. D. Yoshikami for wheat germ tRNA, and Dr. J. C. Rabinowitz for a generous gift of formyltetrahydrofolate synthetase. This investigation was supported by PHS Research Grant No. GM 10791 and Training Grant No. GM 00824.

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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10.1016/0006-291X(70)91025-9

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title = "Protein chain initiation by methionyl-tRNA",

abstract = "Wheat germ contains three chromatographically distinct methionine tRNA's, of which two species, one major and one minor, appear to function in protein chain initiation as demonstrated by the AUG-dependent reaction with puromycin on wheat germ ribosomes. Wheat germ extracts contain a very active transformylase which formylates the minor methionyl-tRNA. The major initiating methionyl-tRNA is not formylated or otherwise modified by wheat germ extracts. We postulate that protein chain initiation in the cytoplasm of wheat germ can be brought about by the major initiating methionyl-tRNA without prior formylation or other modification of the α amino group.",

author = "Leis, {Jonathan P.} and Keller, {Elizabeth B.}",

note = "Funding Information: We wish to thank Mrs. Clara T. Kahn for invaluable assistance in these experiments, Dr. D. Yoshikami for wheat germ tRNA, and Dr. J. C. Rabinowitz for a generous gift of formyltetrahydrofolate synthetase. This investigation was supported by PHS Research Grant No. GM 10791 and Training Grant No. GM 00824.",

year = "1970",

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doi = "10.1016/0006-291X(70)91025-9",

language = "English (US)",

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T1 - Protein chain initiation by methionyl-tRNA

AU - Leis, Jonathan P.

AU - Keller, Elizabeth B.

N1 - Funding Information: We wish to thank Mrs. Clara T. Kahn for invaluable assistance in these experiments, Dr. D. Yoshikami for wheat germ tRNA, and Dr. J. C. Rabinowitz for a generous gift of formyltetrahydrofolate synthetase. This investigation was supported by PHS Research Grant No. GM 10791 and Training Grant No. GM 00824.

PY - 1970/7/27

Y1 - 1970/7/27

N2 - Wheat germ contains three chromatographically distinct methionine tRNA's, of which two species, one major and one minor, appear to function in protein chain initiation as demonstrated by the AUG-dependent reaction with puromycin on wheat germ ribosomes. Wheat germ extracts contain a very active transformylase which formylates the minor methionyl-tRNA. The major initiating methionyl-tRNA is not formylated or otherwise modified by wheat germ extracts. We postulate that protein chain initiation in the cytoplasm of wheat germ can be brought about by the major initiating methionyl-tRNA without prior formylation or other modification of the α amino group.

AB - Wheat germ contains three chromatographically distinct methionine tRNA's, of which two species, one major and one minor, appear to function in protein chain initiation as demonstrated by the AUG-dependent reaction with puromycin on wheat germ ribosomes. Wheat germ extracts contain a very active transformylase which formylates the minor methionyl-tRNA. The major initiating methionyl-tRNA is not formylated or otherwise modified by wheat germ extracts. We postulate that protein chain initiation in the cytoplasm of wheat germ can be brought about by the major initiating methionyl-tRNA without prior formylation or other modification of the α amino group.

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Protein chain initiation by methionyl-tRNA

Abstract

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