Please use this identifier to cite or link to this item: https://doi.org/10.1186/1745-6150-6-57
Title: Not all transmembrane helices are born equal: Towards the extension of the sequence homology concept to membrane proteins
Authors: Wong, W.-C
Maurer-Stroh, S 
Eisenhaber, F 
Keywords: membrane protein
signal peptide
article
biology
chemical phenomena
chemistry
computer program
membrane
protein database
protein secondary structure
protein tertiary structure
sequence alignment
sequence homology
Computational Biology
Databases, Protein
Hydrophobic and Hydrophilic Interactions
Membrane Proteins
Membranes
Protein Sorting Signals
Protein Structure, Secondary
Protein Structure, Tertiary
Sequence Alignment
Sequence Homology, Amino Acid
Software
Issue Date: 2011
Citation: Wong, W.-C, Maurer-Stroh, S, Eisenhaber, F (2011). Not all transmembrane helices are born equal: Towards the extension of the sequence homology concept to membrane proteins. Biology Direct 6 : 57. ScholarBank@NUS Repository. https://doi.org/10.1186/1745-6150-6-57
Abstract: Background: Sequence homology considerations widely used to transfer functional annotation to uncharacterized protein sequences require special precautions in the case of non-globular sequence segments including membrane-spanning stretches composed of non-polar residues. Simple, quantitative criteria are desirable for identifying transmembrane helices (TMs) that must be included into or should be excluded from start sequence segments in similarity searches aimed at finding distant homologues.Results: We found that there are two types of TMs in membrane-associated proteins. On the one hand, there are so-called simple TMs with elevated hydrophobicity, low sequence complexity and extraordinary enrichment in long aliphatic residues. They merely serve as membrane-anchoring device. In contrast, so-called complex TMs have lower hydrophobicity, higher sequence complexity and some functional residues. These TMs have additional roles besides membrane anchoring such as intra-membrane complex formation, ligand binding or a catalytic role. Simple and complex TMs can occur both in single- and multi-membrane-spanning proteins essentially in any type of topology. Whereas simple TMs have the potential to confuse searches for sequence homologues and to generate unrelated hits with seemingly convincing statistical significance, complex TMs contain essential evolutionary information.Conclusion: For extending the homology concept onto membrane proteins, we provide a necessary quantitative criterion to distinguish simple TMs (and a sufficient criterion for complex TMs) in query sequences prior to their usage in homology searches based on assessment of hydrophobicity and sequence complexity of the TM sequence segments.Reviewers: This article was reviewed by Shamil Sunyaev, L. Aravind and Arcady Mushegian. © 2011 Wong et al; licensee BioMed Central Ltd.
Source Title: Biology Direct
URI: https://scholarbank.nus.edu.sg/handle/10635/174178
ISSN: 17456150
DOI: 10.1186/1745-6150-6-57
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