Biogenesis and secretion of alkaline phosphatase and its mutant forms in Escherichia coli. IV. Changes in the signal peptide C-proximal domain affect processing

Z. N. Karamysheva; A. L. Karamyshev; V. N. Ksenzenko; M. G. Shlyapnikov; A. V. Kayawa; M. A. Nesmeyanova

Biogenesis and secretion of alkaline phosphatase and its mutant forms in Escherichia coli. IV. Changes in the signal peptide C-proximal domain affect processing

Z. N. Karamysheva, A. L. Karamyshev, V. N. Ksenzenko, M. G. Shlyapnikov, A. V. Kayawa, M. A. Nesmeyanova

Biological Sciences

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

Abstract

The effect of 57 amino acid substitutions in the C-proximal domain of the Esherichia coli alkaline phosphatase signal peptide on the processing of this protein was studied. Only substitution of aromatic (Phe, Tyr), charged (Lys, His, Glu), or highly polar amino acids into positions -1 and -3, or introduction of Pro at -3 and Leu at -1 completely interrupt processing. The results are a new experimental demonstration of the "-3, -1" rule that describes the processing sites of secreted proteins. It is shown for the first time that the processing efficiency is also determined by the structure of amino acids in positions -2 and -5.

Original language	English
Pages (from-to)	768-774
Number of pages	7
Journal	Molecular Biology
Volume	31
Issue number	5
State	Published - Sep 1997

Keywords

Alkaline phosphatase
Amino acid substitutions
Biogenesis
E. coli
Processing

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title = "Biogenesis and secretion of alkaline phosphatase and its mutant forms in Escherichia coli. IV. Changes in the signal peptide C-proximal domain affect processing",

abstract = "The effect of 57 amino acid substitutions in the C-proximal domain of the Esherichia coli alkaline phosphatase signal peptide on the processing of this protein was studied. Only substitution of aromatic (Phe, Tyr), charged (Lys, His, Glu), or highly polar amino acids into positions -1 and -3, or introduction of Pro at -3 and Leu at -1 completely interrupt processing. The results are a new experimental demonstration of the {"}-3, -1{"} rule that describes the processing sites of secreted proteins. It is shown for the first time that the processing efficiency is also determined by the structure of amino acids in positions -2 and -5.",

keywords = "Alkaline phosphatase, Amino acid substitutions, Biogenesis, E. coli, Processing",

author = "Karamysheva, {Z. N.} and Karamyshev, {A. L.} and Ksenzenko, {V. N.} and Shlyapnikov, {M. G.} and Kayawa, {A. V.} and Nesmeyanova, {M. A.}",

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T1 - Biogenesis and secretion of alkaline phosphatase and its mutant forms in Escherichia coli. IV. Changes in the signal peptide C-proximal domain affect processing

AU - Karamysheva, Z. N.

AU - Karamyshev, A. L.

AU - Ksenzenko, V. N.

AU - Shlyapnikov, M. G.

AU - Kayawa, A. V.

AU - Nesmeyanova, M. A.

PY - 1997/9

Y1 - 1997/9

N2 - The effect of 57 amino acid substitutions in the C-proximal domain of the Esherichia coli alkaline phosphatase signal peptide on the processing of this protein was studied. Only substitution of aromatic (Phe, Tyr), charged (Lys, His, Glu), or highly polar amino acids into positions -1 and -3, or introduction of Pro at -3 and Leu at -1 completely interrupt processing. The results are a new experimental demonstration of the "-3, -1" rule that describes the processing sites of secreted proteins. It is shown for the first time that the processing efficiency is also determined by the structure of amino acids in positions -2 and -5.

AB - The effect of 57 amino acid substitutions in the C-proximal domain of the Esherichia coli alkaline phosphatase signal peptide on the processing of this protein was studied. Only substitution of aromatic (Phe, Tyr), charged (Lys, His, Glu), or highly polar amino acids into positions -1 and -3, or introduction of Pro at -3 and Leu at -1 completely interrupt processing. The results are a new experimental demonstration of the "-3, -1" rule that describes the processing sites of secreted proteins. It is shown for the first time that the processing efficiency is also determined by the structure of amino acids in positions -2 and -5.

KW - Alkaline phosphatase

KW - Amino acid substitutions

KW - Biogenesis

KW - E. coli

KW - Processing

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M3 - Article

AN - SCOPUS:0031323178

SN - 0026-8933

VL - 31

SP - 768

EP - 774

JO - Molecular Biology

JF - Molecular Biology

IS - 5

ER -

Biogenesis and secretion of alkaline phosphatase and its mutant forms in Escherichia coli. IV. Changes in the signal peptide C-proximal domain affect processing

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