The unusual glycine-rich C terminus of the Acinetobacter baumannii RNA chaperone Hfq plays an important role in bacterial physiology

• Published in: The Journal of biological chemistry Vol. 293; no. 35; pp. 13377 - 13388
• Main Authors: Sharma, Atin, Dubey, Vineet, Sharma, Rajnikant, Devnath, Kuldip, Gupta, Vivek Kumar, Akhter, Jawed, Bhando, Timsy, Verma, Aparna, Ambatipudi, Kiran, Sarkar, Mihir, Pathania, Ranjana
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 31.08.2018; American Society for Biochemistry and Molecular Biology
• Subjects: AbsR25; Acinetobacter baumannii - chemistry; Acinetobacter baumannii - growth & development; Acinetobacter baumannii - physiology; Acinetobacter Infections - microbiology; Amino Acid Motifs; bacterial adhesion; Bacterial Proteins - chemistry; Bacterial Proteins - metabolism; biofilm; chaperone; gene regulation; Glycine - chemistry; Glycine - metabolism; Gram negative pathogen; Host Factor 1 Protein - chemistry; Host Factor 1 Protein - metabolism; Humans; intrinsically disordered protein; Microbiology; pathogen; Protein Stability; Protein Structure, Secondary; resistance; RNA binding protein; RNA, Bacterial - metabolism; RNA, Small Untranslated - metabolism; small RNA; Stress, Physiological; virulence factor; intrinsically disordered protein; chaperone; gene regulation; AbsR25; biofilm; RNA binding protein; pathogen; virulence factor; small RNA; bacterial adhesion; Gram negative pathogen; resistance

Acinetobacter baumannii is a Gram-negative nosocomial pathogen that causes soft tissue infections in patients who spend a long time in intensive care units. This recalcitrant bacterium is very well known for developing rapid drug resistance, which is a combined outcome of its natural competence and...