Altschul

Ausmees

Bagchi

Bentley

Bisaglia

Borhani

Bosgraaf

Brown

Cabeen

Charbon

Crick

Cuff

Del Rizzo

Delorenzi

Edgar

Edwards

Finn

Fischetti

Flardh

Fraser

Gabriella H. Kelemen

Gonzalez

Gruber

Harbury

Herrmann

Hicks

Hoiczyk

Holberton

Hornung

Insall

John Walshaw

Karimova

Kyte

Letek

Linding

Lupas

Löwe

Marshall

Mazouni

McDonnell

McLachlan

Michael D. Gillespie

Mihajlovic

Monera

Norrander

Olia

Omura

O’Shea

Parry

Pauling

Peters

Puupponen-Pimiä

Rice

Roberts

Ross

Shin

Smith

Sokolova

Squire

Stetefeld

Strelkov

Sumby

Sweet

The UniProt Consortium

Wade

Walter

Weber

Wilson

Wise

English

Crossref

A novel coiled-coil repeat variant in a class of bacterial cytoskeletal proteins

In recent years, a number of bacterial coiled-coil proteins have been characterised which have roles in cell growth and morphology. Several have been shown to have a cytoskeletal function and some have been proposed to have an IF-like character in particular. We recently demonstrated in Streptomyces coelicolor a cytoskeletal role of Scy, a large protein implicated in filamentous growth, whose sequence is dominated by an unusual coiled-coil repeat. We present a detailed analysis of this 51-residue repeat and conclude that it is likely to form a parallel dimeric non-canonical coiled coil based on hendecads but with regions of local underwinding reflecting highly periodic modifications in the sequence. We also demonstrate that traditional sequence similarity searching is insufficient to identify all but the close orthologues of such repeat-dominated proteins, but that by an analysis of repeat periodicity and composition, remote homologues can be found. One clear candidate, despite a great size discrepancy and unremarkable sequence identity, is the known filament-former FilP in the same species. Both proteins appear distinct from the archetypal bacterial IF-like protein; they therefore may constitute a new class of bacterial filamentous protein. The similar sequence characteristics of both suggest their likely oligomer state and a possible mechanism for higher-order assembly into filaments. Another remote homologue in Actinomyces was highlighted by this method. Further, a known coiled-coil protein, DivIVA, appears to share some of these sequence characteristics

Walshaw, John

Gillespie, Michael D.

Kelemen, Gabriella H.

University of East Anglia digital repository

A novel coiled-coil repeat variant in a class of bacterial cytoskeletal proteins

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University of East Anglia digital repository