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Open AccessJournal ArticleDOI

Patterns of Amino Acids near Signal‐Sequence Cleavage Sites

Gunnar von Heijne
- 01 Jun 1983 - 
- Vol. 133, Iss: 1, pp 17-21
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TLDR
In this paper, some such patterns, based on a sample of 78 eukaryotic signal sequences, are presented and discussed, and a first attempt at formulating rules for the prediction of cleavage sites is made.
Abstract
According to the signal hypothesis, a signal sequence, once having initiated export of a growing protein chain across the rough endoplasmic reticulum, is cleaved from the mature protein at a specific site. It has long been known that some part of the cleavage specificity resides in the last residue of the signal sequence, which invariably is one with a small, uncharged side-chain, but no further specific patterns of amino acids near the point of cleavage have been discovered so far. In this paper, some such patterns, based on a sample of 78 eukaryotic signal sequences, are presented and discussed, and a first attempt at formulating rules for the prediction of cleavage sites is made.

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Citations
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Journal ArticleDOI

A new method for predicting signal sequence cleavage sites.

TL;DR: A new method for identifying secretory signal sequences and for predicting the site of cleavage between a signal sequence and the mature exported protein is described.
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Predicting subcellular localization of proteins based on their N-terminal amino acid sequence.

TL;DR: A neural network-based tool, TargetP, for large-scale subcellular location prediction of newly identified proteins has been developed and it is estimated that 10% of all plant proteins are mitochondrial and 14% chloroplastic, and that the abundance of secretory proteins, in both Arabidopsis and Homo, is around 10%.
Journal ArticleDOI

A combined transmembrane topology and signal peptide prediction method.

TL;DR: Phobius, a combined transmembrane protein topology and signal peptide predictor based on a hidden Markov model, noted a drastic reduction of false classifications compared to TMHMM/SignalP, suggesting that Phobius is well suited for whole-genome annotation of signal peptides and trans Membrane regions.
Journal ArticleDOI

Molecular cloning and expression of human hepatocyte growth factor

TL;DR: The nucleotide sequence of the human HGF cDNA reveals that both α- andβ-chains are contained in a single open reading frame coding for a pre-pro precursor protein of 728 amino acids, which indicates that the activity of HGF is not species-specific.
Journal ArticleDOI

Signal sequences: The limits of variation

TL;DR: The results show subtle differences between eukaryotic and prokaryotic sequences, but the general impression of signal sequences as being highly variable is reinforced.
References
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Journal ArticleDOI

Nucleotide sequence of cloned cDNA for bovine corticotropin-beta-lipotropin precursor.

TL;DR: The nucleotide sequence of a 1,091-base pair cloned cDNA insert encoding bovine corticotropin-β-lipotropin precursor mRNA indicates that the precursor protein consists of repetitive units and includes a third melanotropin sequence in its cryptic portion.
Journal ArticleDOI

Cloning and sequence analysis of cDNA for porcine beta-neo-endorphin/dynorphin precursor

TL;DR: The primary structure of a precursor protein that contains β-neo-endorphin, dynorphin and a third leucine-enkephalin sequence with a carboxyl extension has been deduced from the nucleotide sequence of cloned DNA complementary to the porcine hypothalamic mRNA encoding it.
Journal ArticleDOI

Primary structure of the human Met- and Leu-enkephalin precursor and its mRNA

TL;DR: The nucleotide sequence of a complete cDNA copy of enkephalin precursor mRNA from human phaeochromocytoma is reported and shows that the precursor is 267 amino acids long and contains six interspersed Met-enkephaline sequences and one Leu-encephalin sequence.
Journal ArticleDOI

Translocation of proteins across the endoplasmic reticulum. I. Signal recognition protein (SRP) binds to in-vitro-assembled polysomes synthesizing secretory protein.

TL;DR: High- affinity binding and the selective translation-inhibitory effect of SRP were largely abolished when the leucine (Leu) analogue beta-hydroxyLeu was incorporated into the nascent secretory polypeptide.
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