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SsgA‐like proteins determine the fate of peptidoglycan during sporulation of Streptomyces coelicolor
Author(s) -
Noens Elke E. E.,
Mersinias Vassilis,
Traag Bjørn A.,
Smith Colin P.,
Koerten Henk K.,
van Wezel Gilles P.
Publication year - 2005
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.2005.04883.x
Subject(s) - streptomyces coelicolor , biology , peptidoglycan , cell division , spore , sporogenesis , hypha , cell wall , microbiology and biotechnology , penicillin binding proteins , streptomyces , mutant , genetics , biochemistry , gene , cell , bacteria , bacterial protein
Summary During developmental cell division in sporulation‐committed aerial hyphae of streptomycetes, up to a hundred septa are simultaneously produced, in close harmony with synchromous chromosome condensation and segregation. Several unique protein families are involved in the control of this process in actinomycetes, including that of the SsgA‐like proteins (SALPs). Mutants for each of the individual SALP genes were obtained, and high‐resolution and fluorescence imaging revealed that each plays an important and highly specific role in the control of the sporulation process, and their function relates to the build‐up and degradation of septal and spore‐wall peptidoglycan. While SsgA and SsgB are essential for sporulation‐specific cell division in Streptomyces coelicolor , SsgC–G are responsible for correct DNA segregation/condensation (SsgC), spore wall synthesis (SsgD), autolytic spore separation (SsgE, SsgF) or exact septum localization (SsgG). Our experiments paint a picture of a novel protein family that acts through timing and localization of the activity of penicillin‐binding proteins and autolysins, thus controlling important steps during the initiation and the completion of sporulation in actinomycetes.